RRC ID 53705
Author Yahashiri A, Jorgenson MA, Weiss DS.
Title Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides.
Journal Proc Natl Acad Sci U S A
Abstract Bacterial SPOR domains bind peptidoglycan (PG) and are thought to target proteins to the cell division site by binding to "denuded" glycan strands that lack stem peptides, but uncertainties remain, in part because septal-specific binding has yet to be studied in a purified system. Here we show that fusions of GFP to SPOR domains from the Escherichia coli cell-division proteins DamX, DedD, FtsN, and RlpA all localize to septal regions of purified PG sacculi obtained from E. coli and Bacillus subtilis. Treatment of sacculi with an amidase that removes stem peptides enhanced SPOR domain binding, whereas treatment with a lytic transglycosylase that removes denuded glycans reduced SPOR domain binding. These findings demonstrate unequivocally that SPOR domains localize by binding to septal PG, that the physiologically relevant binding site is indeed a denuded glycan, and that denuded glycans are enriched in septal PG rather than distributed uniformly around the sacculus. Accumulation of denuded glycans in the septal PG of both E. coli and B. subtilis, organisms separated by 1 billion years of evolution, suggests that sequential removal of stem peptides followed by degradation of the glycan backbone is an ancient feature of PG turnover during bacterial cell division. Linking SPOR domain localization to the abundance of a structure (denuded glycans) present only transiently during biogenesis of septal PG provides a mechanism for coordinating the function of SPOR domain proteins with the progress of cell division.
Volume 112(36)
Pages 11347-52
Published 2015-9-8
DOI 10.1073/pnas.1508536112
PII 1508536112
PMID 26305949
PMC PMC4568695
MeSH Amino Acid Sequence Bacillus subtilis / genetics Bacillus subtilis / metabolism Binding Sites / genetics Cell Division Cell Wall / genetics Cell Wall / metabolism Escherichia coli / genetics Escherichia coli / metabolism* Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism* Green Fluorescent Proteins / genetics Green Fluorescent Proteins / metabolism Microscopy, Fluorescence Microscopy, Phase-Contrast Models, Biological Mutation Peptides / metabolism* Peptidoglycan / metabolism* Protein Binding
IF 9.58
Times Cited 41
Prokaryotes E. coli