Influence of Lif, the lysostaphin immunity factor, on acceptors of surface proteins and cell wall sorting efficiency in Staphylococcus carnosus.
Proteins harboring a C-terminal cell wall sorting signal are covalently linked to pentaglycine acceptors within the staphylococcal peptidoglycan. This pentaglycine was modified when the lysostaphin immunity factor (Lif) of Staphylococcus simulans was expressed in Staphylococcus carnosus, likely by the exchange of two glycine residues for serine residues. A reporter protein was efficiently linked to the modified acceptor, indicating that the sorting reaction is not strictly dependent on the wild-type structures of the acceptors.
Strauss
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A
Lehrstuhl für Mikrobielle Genetik, Universität Tübingen, 72076 Tübingen, Germany.
Thumm
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G
Götz
F
F
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D004352:Drug Resistance, Microbial; D005998:Glycine / Q000378:metabolism; D008248:Lysostaphin / Q000494:pharmacology*; D008565:Membrane Proteins / Q000378:metabolism; D010455:Peptides; D013210:Staphylococcus / Q000187:drug effects / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D008565:Membrane Proteins; D010455:Peptides; D008248:Lysostaphin; D005998:Glycine