Discovery and Characterization of Three NewEscherichia coliSeptal Ring Proteins That Contain a SPOR Domain: DamX, DedD, and RlpA
- 1 January 2010
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 192 (1) , 242-255
- https://doi.org/10.1128/jb.01244-09
Abstract
SPOR domains are ∼70 amino acids long and occur in >1,500 proteins identified by sequencing of bacterial genomes. The SPOR domains in the FtsN cell division proteins from Escherichia coli and Caulobacter crescentus have been shown to bind peptidoglycan. Besides FtsN, E. coli has three additional SPOR domain proteins—DamX, DedD, and RlpA. We show here that all three of these proteins localize to the septal ring in E. coli. The loss of DamX or DedD either alone or in combination with mutations in genes encoding other division proteins resulted in a variety of division phenotypes, demonstrating that DamX and DedD participate in cytokinesis. In contrast, RlpA mutants divided normally. Follow-up studies revealed that the SPOR domains themselves localize to the septal ring in vivo and bind peptidoglycan in vitro. Even SPOR domains from heterologous organisms, including Aquifex aeolicus, localized to septal rings when produced in E. coli and bound to purified E. coli peptidoglycan sacculi. We speculate that SPOR domains localize to the division site by binding preferentially to septal peptidoglycan. We further suggest that SPOR domain proteins are a common feature of the division apparatus in bacteria. DamX was characterized further and found to interact with multiple division proteins in a bacterial two-hybrid assay. One interaction partner is FtsQ, and several synthetic phenotypes suggest that DamX is a negative regulator of FtsQ function.This publication has 81 references indexed in Scilit:
- Self-Enhanced Accumulation of FtsN at Division Sites and Roles for Other Proteins with a SPOR Domain (DamX, DedD, and RlpA) in Escherichia coli Cell ConstrictionJournal of Bacteriology, 2009
- ATP-Binding Site Lesions in FtsE Impair Cell DivisionJournal of Bacteriology, 2009
- The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like StructureJournal of Molecular Biology, 2009
- Morphogenesis of rod-shaped sacculiFEMS Microbiology Reviews, 2008
- Role of SufI (FtsP) in Cell Division of Escherichia coli : Evidence for Its Involvement in Stabilizing the Assembly of the DivisomeJournal of Bacteriology, 2007
- Genome Sequence of the Cellulolytic Gliding Bacterium Cytophaga hutchinsoniiApplied and Environmental Microbiology, 2007
- Role for the Nonessential N Terminus of FtsN in Divisome AssemblyJournal of Bacteriology, 2007
- Direct Visualization of Red Fluorescent Lipoproteins Indicates Conservation of the Membrane Sorting Rules in the FamilyEnterobacteriaceaeJournal of Bacteriology, 2006
- Construction of Escherichia coli K‐12 in‐frame, single‐gene knockout mutants: the Keio collectionMolecular Systems Biology, 2006
- Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent proteinNature Biotechnology, 2004