Identification of sortase substrates by specificity profiling

[Display omitted] Sortases catalyze the attachment of surface proteins to the peptidoglycan layer of gram-positive bacteria and further represent powerful tools of protein chemistry. During catalysis sortases cleave a donor substrate containing the LPxTG (x=any amino acid) sorting motif under format...

Full description

Saved in:

Bibliographic Details
Published in:	Bioorganic & medicinal chemistry Vol. 25; no. 18; pp. 5002 - 5007
Main Authors:	Schmohl, Lena, Bierlmeier, Jan, von Kügelgen, Nicolai, Kurz, Leonie, Reis, Pascal, Barthels, Fabian, Mach, Pia, Schutkowski, Mike, Freund, Christian, Schwarzer, Dirk
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 15-09-2017
Subjects:	Amino Acid Sequence Aminoacyltransferases - genetics Aminoacyltransferases - metabolism Bacterial Proteins - genetics Bacterial Proteins - metabolism Chromatography, High Pressure Liquid Cysteine Endopeptidases - genetics Cysteine Endopeptidases - metabolism Mass Spectrometry Peptides - analysis Peptides - metabolism Protein labeling Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sortase Sortase-mediated ligation Spectrometry, Fluorescence Staphylococcus - enzymology Staphylococcus aureus Streptococcus pyogenes Substrate Specificity Streptococcus pyogenes Sortase-mediated ligation Staphylococcus aureus Sortase Protein labeling
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	[Display omitted] Sortases catalyze the attachment of surface proteins to the peptidoglycan layer of gram-positive bacteria and further represent powerful tools of protein chemistry. During catalysis sortases cleave a donor substrate containing the LPxTG (x=any amino acid) sorting motif under formation of an enzyme-bound thioester and ligate this intermediate to an acceptor protein containing an N-terminal glycine residue. In addition to the well-established sortase A of Staphylococcus aureus several homologs of this enzyme have been identified in the genomes of gram-positive bacteria. We have profiled the specificity of seven sortases of Staphylococci and Streptococci origin and observed that sortases of the latter class displayed a more relaxed specificity for donor and acceptor substrates than their Staphylococci counterparts. Streptococci sortases prefer an LPKLG donor substrate sequence compared to the canonical sorting motif LPKTG. These findings might facilitate the use of Streptococci sortases as tools of protein chemistry.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0968-0896 1464-3391
DOI:	10.1016/j.bmc.2017.06.033