Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides

Atsushi Yahashiri; Matthew A Jorgenson; David S Weiss

doi:10.1073/pnas.1508536112

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Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides

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Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides

Atsushi Yahashiri, Matthew A Jorgenson and David S Weiss

Proceedings of the National Academy of Sciences - PNAS, Vol.112(36), pp.11347-11352

09/08/2015

DOI: 10.1073/pnas.1508536112

PMCID: PMC4568695

PMID: 26305949

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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.

Peptidoglycan - metabolism

Amino Acid Sequence

Green Fluorescent Proteins - metabolism

Microscopy, Phase-Contrast

Cell Wall - genetics

Escherichia coli Proteins - metabolism

Green Fluorescent Proteins - genetics

Binding Sites - genetics

Bacillus subtilis - genetics

Peptides - metabolism

Escherichia coli - genetics

Models, Biological

Cell Division

Cell Wall - metabolism

Escherichia coli - metabolism

Escherichia coli Proteins - genetics

Protein Binding

Mutation

Bacillus subtilis - metabolism

Microscopy, Fluorescence

Details

Title: Subtitle: Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides
Creators: Atsushi Yahashiri - Department of Microbiology, Carver College of Medicine, The University of Iowa, Iowa City, IA 52242
Matthew A Jorgenson - Department of Microbiology, Carver College of Medicine, The University of Iowa, Iowa City, IA 52242
David S Weiss - Department of Microbiology, Carver College of Medicine, The University of Iowa, Iowa City, IA 52242 david-weiss@uiowa.edu
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences - PNAS, Vol.112(36), pp.11347-11352
Publisher: United States
DOI: 10.1073/pnas.1508536112
PMID: 26305949
PMCID: PMC4568695
ISSN: 1091-6490
eISSN: 1091-6490
Grant note: GM083975 / NIGMS NIH HHS R01 GM083975 / NIGMS NIH HHS
Language: English
Date published: 09/08/2015
Academic Unit: Microbiology and Immunology
Record Identifier: 9984001206302771

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