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Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE.
Hu Z, Lutkenhaus J. Hu Z, et al. Mol Microbiol. 1999 Oct;34(1):82-90. doi: 10.1046/j.1365-2958.1999.01575.x. Mol Microbiol. 1999. PMID: 10540287
Placement of the Z ring at midcell in Escherichia coli is assured by the action of the min system, which blocks usage of potential division sites that exist at the cell poles. ...Thus, MinC is positioned by the other Min products, but in a dynamic manner so that it is in p …
Placement of the Z ring at midcell in Escherichia coli is assured by the action of the min system, which blocks usage of potential di …
Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction.
Zhou H, Schulze R, Cox S, Saez C, Hu Z, Lutkenhaus J. Zhou H, et al. Among authors: hu z. J Bacteriol. 2005 Jan;187(2):629-38. doi: 10.1128/JB.187.2.629-638.2005. J Bacteriol. 2005. PMID: 15629934 Free PMC article.
The MinD ATPase is critical to the oscillation of the Min proteins, which limits formation of the Z ring to midcell. In the presence of ATP, MinD binds to the membrane and recruits MinC, forming a complex that can destabilize the cytokinetic Z ring. ...
The MinD ATPase is critical to the oscillation of the Min proteins, which limits formation of the Z ring to midcell. In the presence …
Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE.
Hu Z, Gogol EP, Lutkenhaus J. Hu Z, et al. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6761-6. doi: 10.1073/pnas.102059099. Epub 2002 Apr 30. Proc Natl Acad Sci U S A. 2002. PMID: 11983867 Free PMC article.
Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.
Hu Z, Saez C, Lutkenhaus J. Hu Z, et al. J Bacteriol. 2003 Jan;185(1):196-203. doi: 10.1128/jb.185.1.196-203.2003. J Bacteriol. 2003. PMID: 12486056 Free PMC article.
In Escherichia coli, the min system prevents division away from midcell through topological regulation of MinC, an inhibitor of Z-ring formation. ...
In Escherichia coli, the min system prevents division away from midcell through topological regulation of MinC, an inhibitor of Z-rin …
Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ.
Hu Z, Lutkenhaus J. Hu Z, et al. J Bacteriol. 2000 Jul;182(14):3965-71. doi: 10.1128/jb.182.14.3965-3971.2000. J Bacteriol. 2000. PMID: 10869074 Free PMC article.
In Escherichia coli FtsZ assembles into a Z ring at midcell while assembly at polar sites is prevented by the min system. MinC, a component of this system, is an inhibitor of FtsZ assembly that is positioned within the cell by interaction with MinDE. ...The fusion of these …
In Escherichia coli FtsZ assembles into a Z ring at midcell while assembly at polar sites is prevented by the min system. MinC, a com …
The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.
Hu Z, Mukherjee A, Pichoff S, Lutkenhaus J. Hu Z, et al. Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14819-24. doi: 10.1073/pnas.96.26.14819. Proc Natl Acad Sci U S A. 1999. PMID: 10611296 Free PMC article.
Positioning of the Z ring at the midcell site in Escherichia coli is assured by the min system, which masks polar sites through topological regulation of MinC, an inhibitor of division. ...These results, along with MinC localization, suggest that MinC rapidly oscillates be …
Positioning of the Z ring at the midcell site in Escherichia coli is assured by the min system, which masks polar sites through topol …
Molecular analysis of (R)-(+)-mandelonitrile lyase microheterogeneity in black cherry.
Hu Z, Poulton JE. Hu Z, et al. Plant Physiol. 1999 Apr;119(4):1535-46. doi: 10.1104/pp.119.4.1535. Plant Physiol. 1999. PMID: 10198113 Free PMC article.
Like MDL1 and MDL3 cDNAs (Z. Hu, J.E. Poulton [1997] Plant Physiol 115: 1359-1369), they had open reading frames that predicted a flavin adenine dinucleotide-binding site, multiple N-glycosylation sites, and an N-terminal signal sequence. ...
Like MDL1 and MDL3 cDNAs (Z. Hu, J.E. Poulton [1997] Plant Physiol 115: 1359-1369), they had open reading frames that predicte …
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