ArticleJournal of bacteriology2009
Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 67 citations in OpenAlex.
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- Protein-Protein Interaction: Bacterial Two Hybrid.Methods in molecular biology (Clifton, N.J.) · 2024Article
- FliL and its paralog MotF have distinct roles in the stator activity of the Sinorhizobium meliloti flagellar motor.Molecular microbiology · 2022Article
- Bacterial Small Membrane Proteins: the Swiss Army Knife of Regulators at the Lipid Bilayer.Journal of bacteriology · 2022Review
- A Bacterial Two-Hybrid System for In Vivo Assays of Protein-Protein Interactions and Drug Discovery.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Bacterial cell proliferation: from molecules to cells.FEMS microbiology reviews · 2021Review
- DrpB (YedR) Is a Nonessential Cell Division Protein in Escherichia coli.Journal of bacteriology · 2020Article
- Escherichia coli YegI is a novel Ser/Thr kinase lacking conserved motifs that localizes to the inner membrane.FEBS letters · 2020Article
- Single Amino Acid Replacements in RocA Disrupt Protein-Protein Interactions To Alter the Molecular Pathogenesis of Group AInfection and immunity · 2020Article
- Persister Cells Resuscitate Using Membrane Sensors that Activate Chemotaxis, Lower cAMP Levels, and Revive Ribosomes.iScience · 2020Article
- A Bacterial Adenylate Cyclase-Based Two-Hybrid System Compatible with GatewayMethods in molecular biology (Clifton, N.J.) · 2018Article
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- The divisome at 25: the road ahead.Current opinion in microbiology · 2017Review
- Membrane Topology and Structural Insights into the Peptide Pheromone Receptor ComD, A Quorum-Sensing Histidine Protein Kinase of Streptococcus mutans.Scientific reports · 2016Article
- Article
- Characterization of interactions between inclusion membrane proteins from Chlamydia trachomatis.Frontiers in cellular and infection microbiology · 2015Article
- Identification and Partial Characterization of Potential FtsL and FtsQ Homologs of Chlamydia.Frontiers in microbiology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of the Escherichia coli division septum is catalyzed by a number of essential proteins (named Fts) that assemble into a ring-like structure at the future division site. Many of these Fts proteins are intrinsic transmembrane proteins whose functions are largely unknown. In the present study, we attempted to identify a novel putative component(s) of the E. coli cell division machinery by searching for proteins that could interact with known Fts proteins. To do that, we used a bacterial two-hybrid system based on interaction-mediated reconstitution of a cyclic AMP (cAMP) signaling cascade to perform a library screening in order to find putative partners of E. coli cell division protein FtsL. Here we report the characterization of YmgF, a 72-residue integral membrane protein of unknown function that was found to associate with many E. coli cell division proteins and to localize to the E. coli division septum in an FtsZ-, FtsA-, FtsQ-, and FtsN-dependent manner. Although YmgF was previously shown to be not essential for cell viability, we found that when overexpressed, YmgF was able to overcome the thermosensitive phenotype of the ftsQ1(Ts) mutation and restore its viability under low-osmolarity conditions. Our results suggest that YmgF might be a novel component of the E. coli cell division machinery.
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