Division site placement in E.coli: Mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains

EMBO Journal

Volumn 21, Issue 13, 2002, Pages 3347-3357

  Shih, Yu Ling ^a   Fu, Xiaoli ^a   King, Glenn F ^a   Le, Trung ^a   Rothfield, Lawrence ^a  

^a UNIVERSITY OF CONNECTICUT HEALTH CENTER   (United States)

Author keywords

Cell division; CFP; Minicell; Septation; YFP

Indexed keywords

BACTERIAL PROTEIN; GREEN FLUORESCENT PROTEIN; MINC PROTEIN; MIND PROTEIN; PROTEIN MINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BINDING SITE; CELL DIVISION; CELL GROWTH; CONTROLLED STUDY; ESCHERICHIA COLI; GENE MUTATION; MEMBRANE STRUCTURE; MITOSIS INHIBITION; NONHUMAN; OSCILLATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN STRUCTURE;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CELL CYCLE PROTEINS; CELL MEMBRANE; CELL POLARITY; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENES, REPORTER; GREEN FLUORESCENT PROTEINS; LUMINESCENT PROTEINS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHENOTYPE; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036646101     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf323     Document Type: Article

References (23)

1. FACS-optimized mutants of the green fluorescent protein (GFP)
2. Posttranslational chromophore formation in recombinant GFP from E.coli requires oxygen
3. A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E.coli
4. The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site
5. Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
6. The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the E.coli division cycle
7. Dynamic localization cycle of the cell division regulator minE in Escherichia coli
8. Wavelength mutations and posttranslational autoxidation of green fluorescent protein
9. Topological regulation in Escherichia coli involves rapid pole-to-pole oscillation of the division inhibitor MinC under the control of MinD and MinE
10. Topological regulation of cell division in E.coli: Spatiotemporal oscillation of MinD occurs through stimulation of its ATPase activity by MinE and phospholipid
11. The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain
12. Structural basis for the topological specificity function of MinE
13. Use of DNA methyltransferase/endonuclease enzyme combinations for megabase mapping of chromosomes
14. The new gene mukB codes for a 177 kD protein with coiled-coil domains involved in chromosome partition in E.coli
15. Deletion analysis of gene minE which encodes the topological specificity factor of cell division in Escherichia coli
16. The MinE ring: An FtsZ-independent cell structure required for selection of the correct division site in E.coli
17. MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli
18. Rapid pole-to-pole oscillation of a protein required for directing division to the middle of E.coli
19. Bacterial cell division
20. Membrane redistribution of the Escherichia coli MinD protein induced by MinE
21. The green fluorescent protein
22. Relation of the oligomeric structure of MinE to its topological specificity function
23. Proper placement of the E.coli division site requires two functions that are associated with different domains of the MinE protein