Minicell-forming mutants of Escherichia coli: suppression of both DicB- and MinD-dependent division inhibition by inactivation of the minC gene product.
about
The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division siteRapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coliCrystal structure of the bacterial cell division regulator MinDGonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction.MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.Membrane redistribution of the Escherichia coli MinD protein induced by MinE.ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coliProper placement of the Escherichia coli division site requires two functions that are associated with different domains of the MinE proteinMembrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplastsThe CnuK9E H-NS complex antagonizes DNA binding of DicA and leads to temperature-dependent filamentous growth in E. coli.Interaction between FtsZ and inhibitors of cell divisionThe Escherichia coli histone-like protein HU affects DNA initiation, chromosome partitioning via MukB, and cell division via MinCDE.Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli.Identification of Bacillus subtilis genes for septum placement and shape determination.The divIVB region of the Bacillus subtilis chromosome encodes homologs of Escherichia coli septum placement (minCD) and cell shape (mreBCD) determinants.A Prophage-Encoded Small RNA Controls Metabolism and Cell Division in Escherichia coli.Conserved glycines in the C terminus of MinC proteins are implicated in their functionality as cell division inhibitors.Targeting of (D)MinC/MinD and (D)MinC/DicB complexes to septal rings in Escherichia coli suggests a multistep mechanism for MinC-mediated destruction of nascent FtsZ rings.New minC mutations suggest different interactions of the same region of division inhibitor MinC with proteins specific for minD and dicB coinhibition pathways.A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli.YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli.
P2860
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P2860
Minicell-forming mutants of Escherichia coli: suppression of both DicB- and MinD-dependent division inhibition by inactivation of the minC gene product.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on October 1990
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Minicell-forming mutants of Es ...... tion of the minC gene product.
@en
Minicell-forming mutants of Es ...... tion of the minC gene product.
@nl
type
label
Minicell-forming mutants of Es ...... tion of the minC gene product.
@en
Minicell-forming mutants of Es ...... tion of the minC gene product.
@nl
prefLabel
Minicell-forming mutants of Es ...... tion of the minC gene product.
@en
Minicell-forming mutants of Es ...... tion of the minC gene product.
@nl
P2093
P2860
P1476
Minicell-forming mutants of Es ...... tion of the minC gene product.
@en
P2093
P2860
P304
P356
10.1128/JB.172.10.5852-5855.1990
P407
P577
1990-10-01T00:00:00Z