Mycobacterial IHF is a highly dynamic nucleoid-associated protein that assists HupB in organizing chromatin

Nucleoid-associated proteins (NAPs) crucially contribute to organizing bacterial chromatin and regulating gene expression. Among the most highly expressed NAPs are the HU and integration host factor (IHF) proteins, whose functional homologues, HupB and mycobacterial integration host factor (mIHF), a...

Full description

Saved in:
Bibliographic Details
Published in:Frontiers in microbiology Vol. 14; p. 1146406
Main Authors: Hołówka, Joanna, Łebkowski, Tomasz, Feddersen, Helge, Giacomelli, Giacomo, Drużka, Karolina, Makowski, Łukasz, Trojanowski, Damian, Broda, Natalia, Bramkamp, Marc, Zakrzewska-Czerwińska, Jolanta
Format: Journal Article
Language:English
Published: Switzerland Frontiers Media S.A 07-03-2023
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Abstract Nucleoid-associated proteins (NAPs) crucially contribute to organizing bacterial chromatin and regulating gene expression. Among the most highly expressed NAPs are the HU and integration host factor (IHF) proteins, whose functional homologues, HupB and mycobacterial integration host factor (mIHF), are found in mycobacteria. Despite their importance for the pathogenicity and/or survival of tubercle bacilli, the role of these proteins in mycobacterial chromosome organization remains unknown. Here, we used various approaches, including super-resolution microscopy, to perform a comprehensive analysis of the roles of HupB and mIHF in chromosome organization. We report that HupB is a structural agent that maintains chromosome integrity on a local scale, and that the lack of this protein alters chromosome morphology. In contrast, mIHF is a highly dynamic protein that binds DNA only transiently, exhibits susceptibility to the chromosomal DNA topology changes and whose depletion leads to the growth arrest of tubercle bacilli. Additionally, we have shown that depletion of integration host factor (msIHF) leads to chromosome shrinkage and replication inhibition.
AbstractList Nucleoid-associated proteins (NAPs) crucially contribute to organizing bacterial chromatin and regulating gene expression. Among the most highly expressed NAPs are the HU and integration host factor (IHF) proteins, whose functional homologues, HupB and mycobacterial integration host factor (mIHF), are found in mycobacteria. Despite their importance for the pathogenicity and/or survival of tubercle bacilli, the role of these proteins in mycobacterial chromosome organization remains unknown. Here, we used various approaches, including super-resolution microscopy, to perform a comprehensive analysis of the roles of HupB and mIHF in chromosome organization. We report that HupB is a structural agent that maintains chromosome integrity on a local scale, and that the lack of this protein alters chromosome morphology. In contrast, mIHF is a highly dynamic protein that binds DNA only transiently, exhibits susceptibility to the chromosomal DNA topology changes and whose depletion leads to the growth arrest of tubercle bacilli. Additionally, we have shown that depletion of Mycobacterium smegmatis integration host factor (msIHF) leads to chromosome shrinkage and replication inhibition.
Nucleoid-associated proteins (NAPs) crucially contribute to organizing bacterial chromatin and regulating gene expression. Among the most highly expressed NAPs are the HU and integration host factor (IHF) proteins, whose functional homologues, HupB and mycobacterial integration host factor (mIHF), are found in mycobacteria. Despite their importance for the pathogenicity and/or survival of tubercle bacilli, the role of these proteins in mycobacterial chromosome organization remains unknown. Here, we used various approaches, including super-resolution microscopy, to perform a comprehensive analysis of the roles of HupB and mIHF in chromosome organization. We report that HupB is a structural agent that maintains chromosome integrity on a local scale, and that the lack of this protein alters chromosome morphology. In contrast, mIHF is a highly dynamic protein that binds DNA only transiently, exhibits susceptibility to the chromosomal DNA topology changes and whose depletion leads to the growth arrest of tubercle bacilli. Additionally, we have shown that depletion of integration host factor (msIHF) leads to chromosome shrinkage and replication inhibition.
Nucleoid-associated proteins (NAPs) crucially contribute to organizing bacterial chromatin and regulating gene expression. Among the most highly expressed NAPs are the HU and integration host factor (IHF) proteins, whose functional homologues, HupB and mycobacterial integration host factor (mIHF), are found in mycobacteria. Despite their importance for the pathogenicity and/or survival of tubercle bacilli, the role of these proteins in mycobacterial chromosome organization remains unknown. Here, we used various approaches, including super-resolution microscopy, to perform a comprehensive analysis of the roles of HupB and mIHF in chromosome organization. We report that HupB is a structural agent that maintains chromosome integrity on a local scale, and that the lack of this protein alters chromosome morphology. In contrast, mIHF is a highly dynamic protein that binds DNA only transiently, exhibits susceptibility to the chromosomal DNA topology changes and whose depletion leads to the growth arrest of tubercle bacilli. Additionally, we have shown that depletion of Mycobacterium smegmatis integration host factor (msIHF) leads to chromosome shrinkage and replication inhibition.
Author Giacomelli, Giacomo
Drużka, Karolina
Trojanowski, Damian
Bramkamp, Marc
Łebkowski, Tomasz
Hołówka, Joanna
Zakrzewska-Czerwińska, Jolanta
Broda, Natalia
Feddersen, Helge
Makowski, Łukasz
AuthorAffiliation 1 Department of Molecular Microbiology, University of Wrocław , Wrocław , Poland
2 Institute for General Microbiology, Christian-Albrechts-University , Kiel , Germany
AuthorAffiliation_xml – name: 1 Department of Molecular Microbiology, University of Wrocław , Wrocław , Poland
– name: 2 Institute for General Microbiology, Christian-Albrechts-University , Kiel , Germany
Author_xml – sequence: 1
  givenname: Joanna
  surname: Hołówka
  fullname: Hołówka, Joanna
  organization: Department of Molecular Microbiology, University of Wrocław, Wrocław, Poland
– sequence: 2
  givenname: Tomasz
  surname: Łebkowski
  fullname: Łebkowski, Tomasz
  organization: Department of Molecular Microbiology, University of Wrocław, Wrocław, Poland
– sequence: 3
  givenname: Helge
  surname: Feddersen
  fullname: Feddersen, Helge
  organization: Institute for General Microbiology, Christian-Albrechts-University, Kiel, Germany
– sequence: 4
  givenname: Giacomo
  surname: Giacomelli
  fullname: Giacomelli, Giacomo
  organization: Institute for General Microbiology, Christian-Albrechts-University, Kiel, Germany
– sequence: 5
  givenname: Karolina
  surname: Drużka
  fullname: Drużka, Karolina
  organization: Department of Molecular Microbiology, University of Wrocław, Wrocław, Poland
– sequence: 6
  givenname: Łukasz
  surname: Makowski
  fullname: Makowski, Łukasz
  organization: Department of Molecular Microbiology, University of Wrocław, Wrocław, Poland
– sequence: 7
  givenname: Damian
  surname: Trojanowski
  fullname: Trojanowski, Damian
  organization: Department of Molecular Microbiology, University of Wrocław, Wrocław, Poland
– sequence: 8
  givenname: Natalia
  surname: Broda
  fullname: Broda, Natalia
  organization: Department of Molecular Microbiology, University of Wrocław, Wrocław, Poland
– sequence: 9
  givenname: Marc
  surname: Bramkamp
  fullname: Bramkamp, Marc
  organization: Institute for General Microbiology, Christian-Albrechts-University, Kiel, Germany
– sequence: 10
  givenname: Jolanta
  surname: Zakrzewska-Czerwińska
  fullname: Zakrzewska-Czerwińska, Jolanta
  organization: Department of Molecular Microbiology, University of Wrocław, Wrocław, Poland
BackLink https://www.ncbi.nlm.nih.gov/pubmed/36960278$$D View this record in MEDLINE/PubMed
BookMark eNpVkc9vFCEUx4mpsbX2H_BgOHqZlR8jAyejjXU3qfGiiTfCPJgd6gyswJisf71sd21aDvDy5b3ve_B5ic5CDA6h15SsOJfq3TB76FeMML6itBUtEc_QBRWibThhP88exefoKuc7UldLWN1foHMulCCskxfo19c9xN5AccmbCW_WN9hnbPDot-O0x3YfTG2EwwKTi942JucI3hRn8S7F4nzAZTQFV93nkvF62X3CVYxpa4L_68MWw5jibIoPr9DzwUzZXZ3OS_Tj5vP363Vz--3L5vrjbQOtUKVhRL4nnEI3dEJyYjrCgVprqQXhhOMgnVJqUFRaqdpeMqiSBM6pFYNtOb9Em6OvjeZO75KfTdrraLy-F-po2qTi64u0Uq1hpO17Kkyt5BLqXw5SdiC468FVrw9Hr93Sz86CCyWZ6Ynp05vgR72NfzQlhEkqRXV4e3JI8ffictGzz-CmyQQXl6xZpyjvKr9DKjumQoo5Jzc89KFEH6jre-r6QF2fqNeiN48nfCj5z5j_Axx4rIE
CitedBy_id crossref_primary_10_1111_mmi_15287
Cites_doi 10.1073/pnas.0913551107
10.1093/nar/gkab696
10.3390/genes13020278
10.3389/fmicb.2020.00590
10.1038/s41598-021-82295-0
10.1038/s41567-019-0679-1
10.1016/j.ymeth.2016.09.016
10.1146/annurev-cellbio-100814-125211
10.1371/journal.pone.0012551
10.1038/s41598-018-33842-9
10.1016/j.jsb.2006.05.006
10.1046/j.1365-2958.2002.03129.x
10.1016/j.jmb.2006.10.024
10.1128/mSphere.00290-21
10.1016/j.bbagen.2019.07.014
10.1006/jmbi.1995.0648
10.1038/sj.emboj.7600434
10.1128/JB.00044-18
10.1016/j.cub.2013.11.050
10.1128/AAC.00739-19
10.1038/s41598-018-32340-2
10.1038/s41598-017-10421-y
10.1093/nar/gkx1215
10.1371/journal.pgen.1008456
10.1093/nar/gkt095
10.1371/journal.pone.0069985
10.1111/j.1365-2958.2008.06239.x
10.1016/j.csbj.2019.06.010
10.1093/nar/gkab094
10.1128/JB.180.20.5473-5477.1998
10.1021/acs.biochem.5b00447
10.3791/3145
10.1128/mBio.01272-17
10.1093/nar/gkab641
10.1128/mBio.02125-14
10.1128/JB.01625-14
10.1038/ncomms5124
10.1126/science.1204697
10.1038/s41576-019-0185-4
10.1128/AEM.00844-12
10.1111/j.1365-2958.2011.07763.x
10.1111/j.1742-4658.2011.08267.x
10.1016/j.cell.2017.12.027
10.1128/JB.00357-17
10.1371/journal.pone.0016019
10.1371/journal.pone.0049885
10.3389/fmicb.2018.01592
10.1371/journal.pgen.1002123
10.1038/nmicrobiol.2016.274
10.1016/j.molcel.2015.07.020
10.1128/JB.05734-11
10.1038/nrmicro2261
10.1073/pnas.1414207111
10.1099/mic.0.045518-0
10.1007/978-0-387-98141-3
10.1111/mmi.13339
10.1099/ijsem.0.005056
10.1128/JB.00961-12
10.1093/nar/gkr1236
10.1016/j.jsb.2019.107434
ContentType Journal Article
Copyright Copyright © 2023 Hołówka, Łebkowski, Feddersen, Giacomelli, Drużka, Makowski, Trojanowski, Broda, Bramkamp and Zakrzewska-Czerwińska.
Copyright © 2023 Hołówka, Łebkowski, Feddersen, Giacomelli, Drużka, Makowski, Trojanowski, Broda, Bramkamp and Zakrzewska-Czerwińska. 2023 Hołówka, Łebkowski, Feddersen, Giacomelli, Drużka, Makowski, Trojanowski, Broda, Bramkamp and Zakrzewska-Czerwińska
Copyright_xml – notice: Copyright © 2023 Hołówka, Łebkowski, Feddersen, Giacomelli, Drużka, Makowski, Trojanowski, Broda, Bramkamp and Zakrzewska-Czerwińska.
– notice: Copyright © 2023 Hołówka, Łebkowski, Feddersen, Giacomelli, Drużka, Makowski, Trojanowski, Broda, Bramkamp and Zakrzewska-Czerwińska. 2023 Hołówka, Łebkowski, Feddersen, Giacomelli, Drużka, Makowski, Trojanowski, Broda, Bramkamp and Zakrzewska-Czerwińska
DBID NPM
AAYXX
CITATION
7X8
5PM
DOA
DOI 10.3389/fmicb.2023.1146406
DatabaseName PubMed
CrossRef
MEDLINE - Academic
PubMed Central (Full Participant titles)
Directory of Open Access Journals
DatabaseTitle PubMed
CrossRef
MEDLINE - Academic
DatabaseTitleList
PubMed

CrossRef
Database_xml – sequence: 1
  dbid: DOA
  name: Directory of Open Access Journals
  url: http://www.doaj.org/
  sourceTypes: Open Website
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1664-302X
EndPage 1146406
ExternalDocumentID oai_doaj_org_article_994a204bb16a43338c146f887c63ebce
10_3389_fmicb_2023_1146406
36960278
Genre Journal Article
GrantInformation_xml – fundername: Opus 19
  grantid: 2020/37/B/NZ1/00556
– fundername: National Science Centre Sonatina 2
  grantid: 2018/28/C/NZ1/00128
GroupedDBID 53G
5VS
9T4
AAFWJ
AAKDD
ACGFO
ACGFS
ACXDI
ADBBV
ADRAZ
AENEX
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BAWUL
BCNDV
DIK
ECGQY
GROUPED_DOAJ
GX1
HYE
IAO
IEA
IHR
IPNFZ
KQ8
M48
M~E
NPM
O5R
O5S
OK1
PGMZT
RIG
RNS
RPM
AAYXX
CITATION
7X8
5PM
AFPKN
ID FETCH-LOGICAL-c469t-2085031c7f76830a703c1ddd1dc6e6e3c8e999f918d894b82c3c88c331d6fd433
IEDL.DBID RPM
ISSN 1664-302X
IngestDate Tue Oct 22 14:39:05 EDT 2024
Tue Sep 17 21:31:56 EDT 2024
Sat Oct 05 05:18:59 EDT 2024
Thu Nov 21 22:38:17 EST 2024
Wed Oct 16 00:39:13 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Keywords mycobacterial IHF
nucleoid-associated protein
HupB
mycobacteria
bacterial chromosome compaction
Language English
License Copyright © 2023 Hołówka, Łebkowski, Feddersen, Giacomelli, Drużka, Makowski, Trojanowski, Broda, Bramkamp and Zakrzewska-Czerwińska.
This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c469t-2085031c7f76830a703c1ddd1dc6e6e3c8e999f918d894b82c3c88c331d6fd433
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Reviewed by: Valakunja Nagaraja, Indian Institute of Science (IISc), India; Remus T. Dame, Leiden University, Netherlands
These authors have contributed equally to this work
Edited by: Tomohiro Shimada, Meiji University, Japan
This article was submitted to Evolutionary and Genomic Microbiology, a section of the journal Frontiers in Microbiology
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10028186/
PMID 36960278
PQID 2791374066
PQPubID 23479
PageCount 1
ParticipantIDs doaj_primary_oai_doaj_org_article_994a204bb16a43338c146f887c63ebce
pubmedcentral_primary_oai_pubmedcentral_nih_gov_10028186
proquest_miscellaneous_2791374066
crossref_primary_10_3389_fmicb_2023_1146406
pubmed_primary_36960278
PublicationCentury 2000
PublicationDate 2023-03-07
PublicationDateYYYYMMDD 2023-03-07
PublicationDate_xml – month: 03
  year: 2023
  text: 2023-03-07
  day: 07
PublicationDecade 2020
PublicationPlace Switzerland
PublicationPlace_xml – name: Switzerland
PublicationTitle Frontiers in microbiology
PublicationTitleAlternate Front Microbiol
PublicationYear 2023
Publisher Frontiers Media S.A
Publisher_xml – name: Frontiers Media S.A
References Gordon (ref13) 2010; 107
Sharadamma (ref43) 2017; 199
Dame (ref5) 2020; 21
Jong (ref6) 2011; 3145
Pedulla (ref36) 1998; 180
Odermatt (ref31); 209
Macvanin (ref26) 2012; 194
Giacomelli (ref12) 2022; 13
Swinger (ref47) 2007; 365
Wasim (ref58) 2021; 49
Ryan (ref41) 2002; 46
Dame (ref3) 2011; 7
Kołodziej (ref20); 6
Luijsterburg (ref25) 2006; 156
Lioy (ref24) 2018; 172
Odermatt (ref32) 2018; 8
Sharadamma (ref44) 2015; 54
Swiercz (ref46) 2013; 41
Sambrook (ref42) 1989
Bhowmick (ref2) 2014; 5
Espeli (ref8) 2008; 68
Flores-Ríos (ref9) 2019; 17
Whiteford (ref59) 2011; 157
Sharadamma (ref45) 2011; 278
Szafran (ref48) 2018; 9
Verma (ref54) 2019; 15
Rock (ref39) 2017; 2
Mishra (ref28) 2013; 8
Badrinarayanan (ref1) 2015; 31
Wang (ref56) 2011; 333
Wang (ref57) 2014; 24
Tinevez (ref49) 2017; 115
Hołówka (ref16) 2018; 200
Trojanowski (ref51) 2019; 63
Wickham (ref60) 2009
Nanji (ref29) 2019; 1863
Kumar (ref22) 2010; 5
Dame (ref4) 2019; 21
Vis (ref55) 1995; 254
Trojanowski (ref50) 2015; 6
Kołodziej (ref21); 11
Ghosh (ref11) 2016; 100
Gupta (ref14) 2014; 196
Panas (ref35) 2014; 111
Rösch (ref40) 2018; 8
Velmurugu (ref53) 2018; 46
Oren (ref33) 2021; 71
Hołówka (ref15) 2017; 8
Jeon (ref18) 2017; 7
Jeong (ref19) 2012; 78
Oviedo-Bocanegra (ref34) 2021; 49
Ghatak (ref10) 2011; 6
Prieto (ref38) 2012; 40
Odermatt (ref30); 16
Petrushenko (ref37) 2011; 81
Yoshua (ref62) 2021; 49
Valens (ref52) 2004; 23
Marbouty (ref27) 2015; 59
Hołówka (ref17) 2020; 11
Lin (ref23) 2012; 7
Dillon (ref7) 2010; 8
Wolanski (ref61) 2011; 193
References_xml – volume: 107
  start-page: 5154
  year: 2010
  ident: ref13
  article-title: Lsr 2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0913551107
  contributor:
    fullname: Gordon
– volume: 49
  start-page: e112
  year: 2021
  ident: ref34
  article-title: Single molecule/particle tracking analysis program SMTracker 2.0 reveals different dynamics of proteins within the RNA degradosome complex in Bacillus subtilis
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkab696
  contributor:
    fullname: Oviedo-Bocanegra
– volume: 13
  start-page: 278
  year: 2022
  ident: ref12
  article-title: Subcellular dynamics of a conserved bacterial polar scaffold protein
  publication-title: Genes
  doi: 10.3390/genes13020278
  contributor:
    fullname: Giacomelli
– volume: 11
  start-page: 590
  year: 2020
  ident: ref17
  article-title: Nucleoid associated proteins: the small organizers that help to cope with stress
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2020.00590
  contributor:
    fullname: Hołówka
– volume: 11
  start-page: 2910
  ident: ref21
  article-title: Lsr 2, a nucleoid-associated protein influencing mycobacterial cell cycle
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-021-82295-0
  contributor:
    fullname: Kołodziej
– volume: 16
  start-page: 57
  ident: ref30
  article-title: Overlapping and essential roles for molecular and mechanical mechanisms in mycobacterial cell division
  publication-title: Nat. Phys.
  doi: 10.1038/s41567-019-0679-1
  contributor:
    fullname: Odermatt
– volume: 115
  start-page: 80
  year: 2017
  ident: ref49
  article-title: TrackMate: an open and extensible platform for single-particle tracking
  publication-title: Methods
  doi: 10.1016/j.ymeth.2016.09.016
  contributor:
    fullname: Tinevez
– volume: 31
  start-page: 171
  year: 2015
  ident: ref1
  article-title: Bacterial chromosome organization and segregation
  publication-title: Annu. Rev. Cell Dev. Biol.
  doi: 10.1146/annurev-cellbio-100814-125211
  contributor:
    fullname: Badrinarayanan
– volume: 5
  start-page: e12551
  year: 2010
  ident: ref22
  article-title: DNA clasping by mycobacterial HU: the C-terminal region of Hup B mediates increased specificity of DNA binding
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0012551
  contributor:
    fullname: Kumar
– volume: 8
  start-page: 15747
  year: 2018
  ident: ref40
  article-title: SMTracker: a tool for quantitative analysis, exploration and visualization of single-molecule tracking data reveals highly dynamic binding of B. subtilis global repressor AbrB throughout the genome
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-018-33842-9
  contributor:
    fullname: Rösch
– volume: 156
  start-page: 262
  year: 2006
  ident: ref25
  article-title: The architectural role of nucleoid-associated proteins in the organization of bacterial chromatin: a molecular perspective
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2006.05.006
  contributor:
    fullname: Luijsterburg
– volume: 46
  start-page: 113
  year: 2002
  ident: ref41
  article-title: IHF and HU stimulate assembly of pre-replication complexes at Escherichia coli oriC by two different mechanisms
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2002.03129.x
  contributor:
    fullname: Ryan
– volume: 365
  start-page: 1005
  year: 2007
  ident: ref47
  article-title: Structure-based analysis of HU-DNA binding
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2006.10.024
  contributor:
    fullname: Swinger
– volume: 6
  start-page: e00290
  ident: ref20
  article-title: Lsr 2 and Its Novel Paralogue Mediate the Adjustment of Mycobacterium smegmatis to Unfavorable Environmental Conditions
  publication-title: mSphere
  doi: 10.1128/mSphere.00290-21
  contributor:
    fullname: Kołodziej
– volume: 1863
  start-page: 129405
  year: 2019
  ident: ref29
  article-title: Streptomyces IHF uses multiple interfaces to bind DNA
  publication-title: Biochim. Biophys. Acta Gen. Subj.
  doi: 10.1016/j.bbagen.2019.07.014
  contributor:
    fullname: Nanji
– volume: 254
  start-page: 692
  year: 1995
  ident: ref55
  article-title: Solution structure of the HU protein from Bacillus stearothermophilus
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1995.0648
  contributor:
    fullname: Vis
– volume: 23
  start-page: 4330
  year: 2004
  ident: ref52
  article-title: Macrodomain organization of the Escherichia coli chromosome
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7600434
  contributor:
    fullname: Valens
– volume: 200
  start-page: e00044-18
  year: 2018
  ident: ref16
  article-title: The origin of chromosomal replication is asymmetrically positioned on the mycobacterial nucleoid, and the timing of its firing depends on Hup B
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.00044-18
  contributor:
    fullname: Hołówka
– volume: 24
  start-page: 287
  year: 2014
  ident: ref57
  article-title: The SMC condensin complex is required for origin segregation in Bacillus subtilis
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2013.11.050
  contributor:
    fullname: Wang
– volume: 63
  start-page: e00739-19
  year: 2019
  ident: ref51
  article-title: Watching DNA replication inhibitors in action: exploiting time-lapse microfluidic microscopy as a tool for target-drug interaction studies in mycobacterium
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.00739-19
  contributor:
    fullname: Trojanowski
– volume: 8
  start-page: 14214
  year: 2018
  ident: ref32
  article-title: Essential nucleoid associated protein mIHF (Rv1388) controls virulence and housekeeping genes in mycobacterium tuberculosis
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-018-32340-2
  contributor:
    fullname: Odermatt
– volume: 7
  start-page: 11896
  year: 2017
  ident: ref18
  article-title: A ring-polymer model shows how macromolecular crowding controls chromosome-arm organization in Escherichia coli
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-017-10421-y
  contributor:
    fullname: Jeon
– volume: 46
  start-page: 1741
  year: 2018
  ident: ref53
  article-title: Two-step interrogation then recognition of DNA binding site by integration host factor: an architectural DNA-bending protein
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkx1215
  contributor:
    fullname: Velmurugu
– volume: 15
  start-page: e1008456
  year: 2019
  ident: ref54
  article-title: Architecture of the Escherichia coli nucleoid
  publication-title: PLoS Genet.
  doi: 10.1371/journal.pgen.1008456
  contributor:
    fullname: Verma
– volume: 41
  start-page: 4171
  year: 2013
  ident: ref46
  article-title: A novel nucleoid-associated protein specific to the actinobacteria
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkt095
  contributor:
    fullname: Swiercz
– volume: 8
  start-page: e69985
  year: 2013
  ident: ref28
  article-title: Integration host factor of mycobacterium tuberculosis, mIHF, compacts DNA by a bending mechanism
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0069985
  contributor:
    fullname: Mishra
– volume: 68
  start-page: 1418
  year: 2008
  ident: ref8
  article-title: DNA dynamics vary according to macrodomain topography in the E. coli chromosome
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.2008.06239.x
  contributor:
    fullname: Espeli
– volume: 17
  start-page: 746
  year: 2019
  ident: ref9
  article-title: Endogenous and foreign nucleoid-associated proteins of bacteria: occurrence, interactions and effects on Mobile genetic elements and Host’s biology
  publication-title: Comput. Struct. Biotechnol. J.
  doi: 10.1016/j.csbj.2019.06.010
  contributor:
    fullname: Flores-Ríos
– volume: 49
  start-page: 3077
  year: 2021
  ident: ref58
  article-title: A hi-C data-integrated model elucidates E. coli chromosome’s multiscale organization at various replication stages
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkab094
  contributor:
    fullname: Wasim
– volume: 180
  start-page: 5473
  year: 1998
  ident: ref36
  article-title: Characterization of the mIHF gene of Mycobacterium smegmatis
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.180.20.5473-5477.1998
  contributor:
    fullname: Pedulla
– volume-title: Molecular Cloning: A Laboratory Manual
  year: 1989
  ident: ref42
  contributor:
    fullname: Sambrook
– volume: 54
  start-page: 4142
  year: 2015
  ident: ref44
  article-title: Molecular dissection of Mycobacterium tuberculosis integration host factor reveals novel insights into the mode of DNA binding and nucleoid compaction
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.5b00447
  contributor:
    fullname: Sharadamma
– volume: 3145
  year: 2011
  ident: ref6
  article-title: Live cell imaging of Bacillus subtilis and Streptococcus pneumoniae using automated time-lapse microscopy
  publication-title: J. Vis. Exp.
  doi: 10.3791/3145
  contributor:
    fullname: Jong
– volume: 8
  start-page: 8
  year: 2017
  ident: ref15
  article-title: Hup B is a bacterial nucleoid-associated protein with an indispensable eukaryotic-like tail
  publication-title: MBio
  doi: 10.1128/mBio.01272-17
  contributor:
    fullname: Hołówka
– volume: 49
  start-page: 8684
  year: 2021
  ident: ref62
  article-title: Integration host factor bends and bridges DNA in a multiplicity of binding modes with varying specificity
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkab641
  contributor:
    fullname: Yoshua
– volume: 6
  start-page: e02125
  year: 2015
  ident: ref50
  article-title: Choreography of the mycobacterium replication machinery during the cell cycle
  publication-title: MBio
  doi: 10.1128/mBio.02125-14
  contributor:
    fullname: Trojanowski
– volume: 196
  start-page: 2646
  year: 2014
  ident: ref14
  article-title: Hup B, a nucleoid-associated protein of mycobacterium tuberculosis, is modified by serine/threonine protein kinases in vivo
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.01625-14
  contributor:
    fullname: Gupta
– volume: 5
  start-page: 4124
  year: 2014
  ident: ref2
  article-title: Targeting mycobacterium tuberculosis nucleoid-associated protein HU with structure-based inhibitors
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms5124
  contributor:
    fullname: Bhowmick
– volume: 333
  start-page: 1445
  year: 2011
  ident: ref56
  article-title: Chromosome organization by a nucleoid-associated protein in live bacteria
  publication-title: Science
  doi: 10.1126/science.1204697
  contributor:
    fullname: Wang
– volume: 21
  start-page: 227
  year: 2020
  ident: ref5
  article-title: Chromosome organization in bacteria: mechanistic insights into genome structure and function
  publication-title: Nat. Rev. Genet.
  doi: 10.1038/s41576-019-0185-4
  contributor:
    fullname: Dame
– volume: 78
  start-page: 5440
  year: 2012
  ident: ref19
  article-title: One-step sequence- and ligation-independent cloning as a rapid and versatile cloning method for functional genomics studies
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.00844-12
  contributor:
    fullname: Jeong
– volume: 81
  start-page: 881
  year: 2011
  ident: ref37
  article-title: A new family of bacterial condensins
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.2011.07763.x
  contributor:
    fullname: Petrushenko
– volume: 278
  start-page: 3447
  year: 2011
  ident: ref45
  article-title: Synergy between the N-terminal and C-terminal domains of Mycobacterium tuberculosis HupB is essential for high-affinity binding, DNA supercoiling and inhibition of RecA-promoted strand exchange
  publication-title: FEBS J.
  doi: 10.1111/j.1742-4658.2011.08267.x
  contributor:
    fullname: Sharadamma
– volume: 172
  start-page: 771
  year: 2018
  ident: ref24
  article-title: Multiscale structuring of the E. coli chromosome by nucleoid-associated and condensin proteins
  publication-title: Cells
  doi: 10.1016/j.cell.2017.12.027
  contributor:
    fullname: Lioy
– volume: 199
  start-page: e00357
  year: 2017
  ident: ref43
  article-title: Defining the functionally important domain and amino acid residues in mycobacterium tuberculosis integration host factor for genome stability, DNA binding, and integrative recombination
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.00357-17
  contributor:
    fullname: Sharadamma
– volume: 6
  start-page: e16019
  year: 2011
  ident: ref10
  article-title: Unveiling the role of Dps in the organization of mycobacterial nucleoid
  publication-title: PloS One
  doi: 10.1371/journal.pone.0016019
  contributor:
    fullname: Ghatak
– volume: 7
  start-page: e49885
  year: 2012
  ident: ref23
  article-title: Physical organization of DNA by multiple non-specific DNA-binding modes of integration host factor (IHF)
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0049885
  contributor:
    fullname: Lin
– volume: 9
  start-page: 1592
  year: 2018
  ident: ref48
  article-title: Amsacrine derivatives selectively inhibit mycobacterial topoisomerase I (TopA), impair M. smegmatis growth and disturb chromosome replication
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2018.01592
  contributor:
    fullname: Szafran
– volume: 7
  start-page: e1002123
  year: 2011
  ident: ref3
  article-title: Chromosomal macrodomains and associated proteins: implications for DNA organization and replication in gram negative bacteria
  publication-title: PLoS Genet.
  doi: 10.1371/journal.pgen.1002123
  contributor:
    fullname: Dame
– volume: 2
  start-page: 16274
  year: 2017
  ident: ref39
  article-title: Programmable transcriptional repression in mycobacteria using an orthogonal CRISPR interference platform
  publication-title: Nat. Microbiol.
  doi: 10.1038/nmicrobiol.2016.274
  contributor:
    fullname: Rock
– volume: 59
  start-page: 588
  year: 2015
  ident: ref27
  article-title: Condensin- and replication-mediated bacterial chromosome folding and origin condensation revealed by hi-C and super-resolution imaging
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2015.07.020
  contributor:
    fullname: Marbouty
– volume: 193
  start-page: 6358
  year: 2011
  ident: ref61
  article-title: The level of AdpA directly affects expression of developmental genes in Streptomyces coelicolor
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.05734-11
  contributor:
    fullname: Wolanski
– volume: 21
  start-page: 227
  year: 2019
  ident: ref4
  article-title: Chromosome organization in bacteria: mechanistic insights into genome structure and function
  publication-title: Nat. Rev. Genet.
  doi: 10.1038/s41576-019-0185-4
  contributor:
    fullname: Dame
– volume: 8
  start-page: 185
  year: 2010
  ident: ref7
  article-title: Bacterial nucleoid-associated proteins, nucleoid structure and gene expression
  publication-title: Nat. Rev. Microbiol.
  doi: 10.1038/nrmicro2261
  contributor:
    fullname: Dillon
– volume: 111
  start-page: 13264
  year: 2014
  ident: ref35
  article-title: Noncanonical SMC protein in Mycobacterium smegmatis restricts maintenance of Mycobacterium fortuitum plasmids
  publication-title: Proc. Natl. Acad. Sci.
  doi: 10.1073/pnas.1414207111
  contributor:
    fullname: Panas
– volume: 157
  start-page: 327
  year: 2011
  ident: ref59
  article-title: Deletion of the histone-like protein (Hlp) from Mycobacterium smegmatis results in increased sensitivity to UV exposure, freezing and isoniazid
  publication-title: Microbiol. Read. Engl.
  doi: 10.1099/mic.0.045518-0
  contributor:
    fullname: Whiteford
– volume-title: In Getting Started With qplot BT-ggplot2: Elegant Graphics for Data Analysis
  year: 2009
  ident: ref60
  doi: 10.1007/978-0-387-98141-3
  contributor:
    fullname: Wickham
– volume: 100
  start-page: 577
  year: 2016
  ident: ref11
  article-title: Lysine acetylation of the mycobacterium tuberculosis HU protein modulates its DNA binding and genome organization
  publication-title: Mol. Microbiol.
  doi: 10.1111/mmi.13339
  contributor:
    fullname: Ghosh
– volume: 71
  start-page: 005056
  year: 2021
  ident: ref33
  article-title: Valid publication of the names of forty-two phyla of prokaryotes
  publication-title: Int. J. Syst. Evol. Microbiol.
  doi: 10.1099/ijsem.0.005056
  contributor:
    fullname: Oren
– volume: 194
  start-page: 6046
  year: 2012
  ident: ref26
  article-title: Noncoding RNAs binding to the nucleoid protein HU in Escherichia coli
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.00961-12
  contributor:
    fullname: Macvanin
– volume: 40
  start-page: 3524
  year: 2012
  ident: ref38
  article-title: Genomic analysis of DNA binding and gene regulation by homologous nucleoid-associated proteins IHF and HU in Escherichia coli K12
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkr1236
  contributor:
    fullname: Prieto
– volume: 209
  start-page: 107434
  ident: ref31
  article-title: Structural and DNA binding properties of mycobacterial integration host factor mIHF
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2019.107434
  contributor:
    fullname: Odermatt
SSID ssj0000402000
Score 2.3903563
Snippet Nucleoid-associated proteins (NAPs) crucially contribute to organizing bacterial chromatin and regulating gene expression. Among the most highly expressed NAPs...
SourceID doaj
pubmedcentral
proquest
crossref
pubmed
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
StartPage 1146406
SubjectTerms bacterial chromosome compaction
HupB
Microbiology
mycobacteria
mycobacterial IHF
nucleoid-associated protein
SummonAdditionalLinks – databaseName: Directory of Open Access Journals
  dbid: DOA
  link: http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Nb9QwELWgEhIXVMrXUqhciRsKJLFx7GMLXW0P5QJI3Cx77GgjULLaj8P213fGTle7CIkLV8eRnXkZz4xsv8fYO6991YgGCgrnhYy1KUxsZeExumglXAstXU6efWu-_tRfrogmZyf1RWfCMj1wNtxHY6SrS-l9pZwUWFAB-naLrgFKRA8xrb6l2ium0hpMZVFZ5lsy-JJBmDrwH0gsPNHjSpI42otEibD_b1nmn4cl96LP9Jg9GdNGfpGn-5Q9iP0Je5SFJLfP2K-bLaBjJuJl7HY9m_JuxR0nMuLfWx6y7Dzvibx46ELhRlBi4Imooev5eu7WHNsR9hWfbRaXHBuz5tMthjcO8-VA2W3_nP2YXn3_PCtGGYUCsPZdF6TCia4LTYulhSgd-jhUIYQqgIoqCtARs8TWVDpoI72uAZs0CFEF1Qa0-Qt21A99fMW4r1WDpsMkTmNlpZVWRrS1giDBmE9OTtj7e5PaRWbLsFhlEAA2AWAJADsCMGGXZPVdT2K6Tg34cXbE3_4L_wk7v8fMomfQdofr47BZ2boxlWhwHBzoZcZwNxSpGNKe64TpA3QP5nL4pO_miX2bOGuJBvD1_5j9KXtMFkmH2po37Gi93MS37OEqbM7SD30H2Jn6Vg
  priority: 102
  providerName: Directory of Open Access Journals
Title Mycobacterial IHF is a highly dynamic nucleoid-associated protein that assists HupB in organizing chromatin
URI https://www.ncbi.nlm.nih.gov/pubmed/36960278
https://search.proquest.com/docview/2791374066
https://pubmed.ncbi.nlm.nih.gov/PMC10028186
https://doaj.org/article/994a204bb16a43338c146f887c63ebce
Volume 14
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lj9MwELboSkhcEG_KY2UkbihtE3sd-8guW5XDIiRA4mbZY0eN2HWrbXsov54ZJ1m1iBNXJ5ad-TyemXj8DWPvvfZlLWooyJwXMlamMLGRhUfropVwDTR0OXnxrf7yU3-6JJocNdyFyUn74NtJur6ZpHaZcyvXNzAd8sSmX68uiDaUmNimIzZC5_AgRs_7L4VEs1l3QwYjMIMQteAnVCg8U-NKKm90YIUyWf-_PMy_EyUPLM_8EXvYu4z8Yze1x-xeTE_Y_a6I5P4p-3W1B1TKTLqMr31ezHm74Y4TEfH1noeu5DxPRFy8akPhekBi4JmkoU18u3Rbju0I-YYvdutzjo1dvaffaNo4LG9X5NmmZ-zH_PL7xaLoSygUgHHvtqAKnKi2UDcYVoiZQ_2GMoRQBlBRRQE6oofYmFIHbaTXFWCTBiHKoJoghXjOTtIqxZeM-0rVKDp04DRGVVppZURTKQgSjDlzcsw-DCK1644pw2KEQQDYDIAlAGwPwJidk9Tv3iSW69yAH2d7rK0x0lUz6X2pHM5FaMDODW6LoET0EMfs3YCZRa2gow6X4mq3sVVtSlHjODjQiw7Du6GogiGdt46ZPkL3aC7HT3AhZubtYeG9-v-ur9kDkkNOY6vfsJPt7S6-ZaNN2J3m_wGneTH_Afrd-q8
link.rule.ids 230,315,729,782,786,866,887,2106,27933,27934,53800,53802
linkProvider National Library of Medicine
linkToHtml http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fb9MwELbYEGIvjF9jZQOMxBtKm8TBsR_ZWJWJdUJiSLxZ8dlRI7a0WtuH8tdz5yRTO_G013MsO_58vjv5_B1jn6yySS5yiMicR5lPdaR9lUUWrYuSoqygosfJxc_88rf6dkY0ObJ_CxOS9sHWw-b6ZtjU05BbOb-BUZ8nNvoxOSXaUGJiG-2wx6iwcbwRpYcTmIKiOG7fyGAMphGkGuyQSoUHctyMChxt2KFA1_8_H_N-quSG7RnvP3TWz9mzztvkX9v2F-yRb16yJ239yfUr9meyBtTnwNeMn50XY14veMmJw_h6zV1brZ43xHk8q11Udlh6xwO_Q93w5bRccpTjblnwYjU_4ShsS0X9RavIYXo7I6e4ec1-jc-uTouoq74QAYbMy4iKd6LGQ15hRCLiEo8GSJxziQPppRegPDqXlU6UUzqzKgUUKRAicbJymRAHbLeZNf6QcZvKHNccfT-FAZmSSmpRpRJcBlp_KbMB-9xjYeYtyYbB4ISQMwE5Q8iZDrkBOyG47r4kguwgwJ8z3YIbrbMyjTNrE1niXIQC7FzhiQpSeAt-wD72YBtUKLolKRs_Wy1MmutE5DgODvSmBf9uKCp-SFe1A6a2tsXWXLZbcDcE0u4e_bcP7_qBPS2uJhfm4vzy-xHbozUJ2XD5Mdtd3q78O7azcKv3QRf-Acc0D3w
linkToPdf http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3db9MwELfYEIgXxjeFAUbiDaVNYuPYvO2r6gSbJgESb1Z8dtSILa3W9qH89dw5ydSiPcGrY8uOf3e-O_n8O8Y-OO2yQhSQkDlPZMhNYkIlE4fWRStRVlDR4-TJt-L8pz4-IZqcz_1bmJi0D64eNpdXw6aextzK-RWM-jyx0cXZEdGGEhPbaO6r0Q67i0qb5huRejyFKTBK0_adDMZhBoGqwQ2pXHgkyJVU5GjDFkXK_tv8zL_TJTfsz3jvf1b-iD3svE5-0PZ5zO6E5gm719ahXD9lv87WgHodeZux2-lkzOsFLzlxGV-uuW-r1vOGuI9ntU_KDtPgeeR5qBu-nJZLju0oNQs-Wc0POTa2JaN-o3XkML2ekXPcPGM_xiffjyZJV4UhAQydlwkV8UTNh6LCyESkJR4RkHnvMw8qqCBAB3QyK5Npr410Ogds0iBE5lXlpRDP2W4za8JLxl2uCtx39AE1BmZaaWVElSvwEoz5VMoB-9jjYect2YbFIIXQsxE9S-jZDr0BOyTIbnoSUXZswJ-z3aZbY2SZp9K5TJW4FqEBB1d4soISwUEYsPc94BYVi25LyibMVgubFyYTBc6DE71oBeBmKiqCSFe2A6a3RGNrLdtfUCIieXcvAa_-feg7dv_ieGy_np5_ec0e0JbEpLhin-0ur1fhDdtZ-NXbqA5_AE4yEfw
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Mycobacterial+IHF+is+a+highly+dynamic+nucleoid-associated+protein+that+assists+HupB+in+organizing+chromatin&rft.jtitle=Frontiers+in+microbiology&rft.au=Ho%C5%82%C3%B3wka%2C+Joanna&rft.au=%C5%81ebkowski%2C+Tomasz&rft.au=Feddersen%2C+Helge&rft.au=Giacomelli%2C+Giacomo&rft.date=2023-03-07&rft.issn=1664-302X&rft.eissn=1664-302X&rft.volume=14&rft.spage=1146406&rft.epage=1146406&rft_id=info:doi/10.3389%2Ffmicb.2023.1146406&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1664-302X&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1664-302X&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1664-302X&client=summon