A sweet new role for LCP enzymes in protein glycosylation
- Univ. of California, Los Angeles, CA (United States)
Summary The peptidoglycan that surrounds G ram‐positive bacteria is affixed with a range of macromolecules that enable the microbe to effectively interact with its environment. Distinct enzymes decorate the cell wall with proteins and glycopolymers. Sortase enzymes covalently attach proteins to the peptidoglycan, while LytR ‐ CpsA ‐ Psr ( LCP ) proteins are thought to attach teichoic acid polymers and capsular polysaccharides. Ton‐That and colleagues have discovered a new glycosylation pathway in the oral bacterium A ctinomyces oris in which sortase and LCP enzymes operate on the same protein substrate. The A . oris LCP protein has a novel function, acting on the cell surface to transfer glycan macromolecules to a protein, which is then attached to the cell wall by a sortase. The reactions are tightly coupled, as elimination of the sortase causes the lethal accumulation of glycosylated protein in the membrane. Since sortase enzymes are attractive drug targets, this novel finding may provide a convenient cell‐based tool to discover inhibitors of this important enzyme family.
- Research Organization:
- Univ. of California, Los Angeles, CA (United States)
- Sponsoring Organization:
- USDOE
- Grant/Contract Number:
- FC03-87ER60615; DE‐FC‐03‐87ER60615
- OSTI ID:
- 1344913
- Alternate ID(s):
- OSTI ID: 1400667
- Journal Information:
- Molecular Microbiology, Vol. 94, Issue 6; ISSN 0950-382X
- Publisher:
- WileyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
Interacting proteins of the essential two-component system YycFG in Bacillus subtilis
|
journal | July 2019 |
Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site
|
journal | October 2016 |
Similar Records
O‐glycosylation effects on family 1 carbohydrate‐binding module solution structures
Listeria monocytogenes wall teichoic acid decoration in virulence and cell‐to‐cell spread