Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 25, Issue 18, Pages 5002-5007Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2017.06.033
Keywords
Sortase-mediated ligation; Protein labeling; Staphylococcus aureus; Streptococcus pyogenes; Sortase
Funding
- Deutsche Forschungsgemeinschaft [SCHW 1163/7-1, FR1325/15-1, SPP 1623]
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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. (C) 2017 Elsevier Ltd. All rights reserved.
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