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A sweet new role for LCP enzymes in protein glycosylation

Journal Article · · Molecular Microbiology
DOI:https://doi.org/10.1111/mmi.12825· OSTI ID:1344913
 [1];  [2]
  1. Univ. of California, Los Angeles, CA (United States); DOE Office of Scientific and Technical Information (OSTI)
  2. Univ. of California, Los Angeles, CA (United States)
+ Show Author Affiliations
The peptidoglycan that surrounds Gram-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 LytRCpsA-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 Actinomyces 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. Furthermore, 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
OSTI ID:
1344913
Alternate ID(s):
OSTI ID: 1400667
Journal Information:
Molecular Microbiology, Journal Name: Molecular Microbiology Journal Issue: 6 Vol. 94; ISSN 0950-382X
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (2)

Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site journal October 2016
Interacting proteins of the essential two-component system YycFG in Bacillus subtilis journal July 2019

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Figure 1(p. 6)figure Figure 1

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