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...
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Published in: | Frontiers in microbiology Vol. 14; p. 1146406 |
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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. |
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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 |
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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 |
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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 |
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Keywords | mycobacterial IHF nucleoid-associated protein HupB mycobacteria bacterial chromosome compaction |
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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 |
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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 |
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