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PMID:15546671

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Citation

Ton-That, H, Marraffini, LA and Schneewind, O (2004) Protein sorting to the cell wall envelope of Gram-positive bacteria. Biochim. Biophys. Acta 1694:269-78

Abstract

The covalent anchoring of surface proteins to the cell wall envelope of Gram-positive bacteria occurs by a universal mechanism requiring sortases, extracellular transpeptidases that are positioned in the plasma membrane. Surface protein precursors are first initiated into the secretory pathway of Gram-positive bacteria via N-terminal signal peptides. C-terminal sorting signals of surface proteins, bearing an LPXTG motif or other recognition sequences, provide for sortase-mediated cleavage and acyl enzyme formation, a thioester linkage between the active site cysteine residue of sortase and the C-terminal carboxyl group of cleaved surface proteins. During cell wall anchoring, sortase acyl enzymes are resolved by the nucleophilic attack of peptidoglycan substrates, resulting in amide bond formation between the C-terminal end of surface proteins and peptidoglycan cross-bridges within the bacterial cell wall envelope. The genomes of Gram-positive bacteria encode multiple sortase genes. Recent evidence suggests that sortase enzymes catalyze protein anchoring reactions of multiple different substrate classes with different sorting signal motif sequences, protein linkage to unique cell wall anchor structures as well as protein polymerization leading to the formation of pili on the surface of Gram-positive bacteria.

Links

PubMed Online version:10.1016/j.bbamcr.2004.04.014

Keywords

Aminoacyltransferases/metabolism; Bacterial Proteins/metabolism; Cell Wall/metabolism; Cysteine Endopeptidases; Fimbriae, Bacterial/metabolism; Gram-Positive Bacteria/physiology; Hyphae/metabolism; Protein Sorting Signals; Protein Transport/physiology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

STRCO:Q9AD92

GO:0043581: mycelium development

ECO:0000315:

P

Figure 7. Shows that ChpH is expressed during mycelium formation, these proteins are presumed to form a film that reduces water surface tension and allows hyphal protrusion into the air

complete
CACAO 5985

STRCO:Q9X9Z2

GO:0043581: mycelium development

ECO:0000315:

P

Figure 7. Shows that ChpE is expressed during mycelium formation, these proteins are presumed to form a film that reduces water surface tension and allows hyphal protrusion into the air.

complete
CACAO 5984


See also

References

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