ArticleJournal of bacteriology2002
Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed.
- Cell constriction requires processive septal peptidoglycan synthase movement independent of FtsZ treadmilling in Staphylococcus aureus.Nature microbiology · 2024Article
- FtsA acts through FtsW to promote cell wall synthesis during cell division inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Topology of the l-Arginine Exporter ArgO Conforms to an Nin-Cout Configuration in Escherichia coli: Requirement for the Cytoplasmic N-Terminal Domain, Functional Helical Interactions, and an Aspartate Pair for ArgO Function.Journal of bacteriology · 2016Article
- FtsZ does not initiate membrane constriction at the onset of division.Scientific reports · 2016Article
- The Escherichia coli membrane protein insertase YidC assists in the biogenesis of penicillin binding proteins.Journal of bacteriology · 2015Article
- Identification and Partial Characterization of Potential FtsL and FtsQ Homologs of Chlamydia.Frontiers in microbiology · 2015Article
- Inactivation of the bacterial RNA polymerase due to acquisition of secondary structure by the ω subunit.The Journal of biological chemistry · 2013Article
- Fine-mapping the contact sites of the Escherichia coli cell division proteins FtsB and FtsL on the FtsQ protein.The Journal of biological chemistry · 2013Article
- Article
- A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex.BMC structural biology · 2011Article
- Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B.Journal of bacteriology · 2010Article
- Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.Biochemistry · 2010Article
- Essential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter spp.Microbiology and molecular biology reviews : MMBR · 2010Review
- Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins.Journal of bacteriology · 2009Article
- Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery.Journal of bacteriology · 2009Article
- Complex regulatory pathways coordinate cell-cycle progression and development in Caulobacter crescentus.Advances in microbial physiology · 2009Review
- Artificial septal targeting of Bacillus subtilis cell division proteins in Escherichia coli: an interspecies approach to the study of protein-protein interactions in multiprotein complexes.Journal of bacteriology · 2008Article
- Roles of pneumococcal DivIB in cell division.Journal of bacteriology · 2008Article
- Contribution of the FtsQ transmembrane segment to localization to the cell division site.Journal of bacteriology · 2007Article
- Mutants, suppressors, and wrinkled colonies: mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
FtsQ, a 276-amino-acid, bitopic membrane protein, is one of the nine proteins known to be essential for cell division in gram-negative bacterium Escherichia coli. To define residues in FtsQ critical for function, we performed random mutagenesis on the ftsQ gene and identified four alleles (ftsQ2, ftsQ6, ftsQ15, and ftsQ65) that fail to complement the ftsQ1(Ts) mutation at the restrictive temperature. Two of the mutant proteins, FtsQ6 and FtsQ15, are functional at lower temperatures but are unable to localize to the division site unless wild-type FtsQ is depleted, suggesting that they compete poorly with the wild-type protein for septal targeting. The other two mutants, FtsQ2 and FtsQ65, are nonfunctional at all temperatures tested and have dominant-negative effects when expressed in an ftsQ1(Ts) strain at the permissive temperature. FtsQ2 and FtsQ65 localize to the division site in the presence or absence of endogenous FtsQ, but they cannot recruit downstream cell division proteins, such as FtsL, to the septum. These results suggest that FtsQ2 and FtsQ65 compete efficiently for septal targeting but fail to promote the further assembly of the cell division machinery. Thus, we have separated the localization ability of FtsQ from its other functions, including recruitment of downstream cell division proteins, and are beginning to define regions of the protein responsible for these distinct capabilities.
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