The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division

Atsushi Yahashiri; Matthew A Jorgenson; David S Weiss

doi:10.1128/jb.00118-17

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The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division

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The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division

Atsushi Yahashiri, Matthew A Jorgenson and David S Weiss

Journal of bacteriology, Vol.199(14), e00118-17

07/15/2017

DOI: 10.1128/jb.00118-17

PMCID: PMC5494741

PMID: 28396350

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Abstract

Sporulation-related repeat (SPOR) domains are small peptidoglycan (PG) binding domains found in thousands of bacterial proteins. The name "SPOR domain" stems from the fact that several early examples came from proteins involved in sporulation, but SPOR domain proteins are quite diverse and contribute to a variety of processes that involve remodeling of the PG sacculus, especially with respect to cell division. SPOR domains target proteins to the division site by binding to regions of PG devoid of stem peptides ("denuded" glycans), which in turn are enriched in septal PG by the intense, localized activity of cell wall amidases involved in daughter cell separation. This targeting mechanism sets SPOR domain proteins apart from most other septal ring proteins, which localize via protein-protein interactions. In addition to SPOR domains, bacteria contain several other PG-binding domains that can exploit features of the cell wall to target proteins to specific subcellular sites.

Cell Division - physiology

Peptidoglycan - metabolism

Bacteria - metabolism

Bacteria - cytology

Protein Binding

Protein Domains

Bacterial Proteins - metabolism

Bacteria - genetics

Protein Transport

Details

Title: Subtitle: The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division
Creators: Atsushi Yahashiri - Department of Microbiology, Carver College of Medicine, The University of Iowa, Iowa City, Iowa, USA
Matthew A Jorgenson - Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA
David S Weiss - Department of Microbiology, Carver College of Medicine, The University of Iowa, Iowa City, Iowa, USA david-weiss@uiowa.edu
Resource Type: Journal article
Publication Details: Journal of bacteriology, Vol.199(14), e00118-17
Publisher: United States
DOI: 10.1128/jb.00118-17
PMID: 28396350
PMCID: PMC5494741
ISSN: 1098-5530
eISSN: 1098-5530
Grant note: name: Internal University of Iowa Funding, award: No number
Language: English
Date published: 07/15/2017
Academic Unit: Microbiology and Immunology
Record Identifier: 9984001129402771

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