Mapping the MinE Site Involved in Interaction with the MinD Division Site Selection Protein of Escherichia Coli

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 2003 Aug 5

PMID 12897015

Citations 31

Authors

Lu-Yan Ma

Glenn King

Lawrence Rothfield

Affiliations

Soon will be listed here.

Abstract

Interactions between the MinD and MinE proteins are required for proper placement of the Escherichia coli division septum. The site within MinE that is required for interaction with MinD was mapped by studying the effects of site-directed minE mutations on MinD-MinE interactions in yeast two-hybrid and three-hybrid experiments. This confirmed that the MinE N-terminal domain is responsible for the interaction of MinE with MinD. Mutations that interfered with the interaction defined an extended surface on one face of the alpha-helical region of the MinE N-terminal domain, consistent with the idea that the MinE-MinD interaction involves formation of a coiled-coil structure by interaction with a complementary helical surface within MinD.

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References

Raskin D, de Boer P . Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc Natl Acad Sci U S A. 1999; 96(9):4971-6. PMC: 21801. DOI: 10.1073/pnas.96.9.4971. View

King G, Rowland S, Pan B, Mackay J, Mullen G, Rothfield L . The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain. Mol Microbiol. 1999; 31(4):1161-9. DOI: 10.1046/j.1365-2958.1999.01256.x. View

Rowland S, Fu X, Sayed M, Zhang Y, Cook W, Rothfield L . Membrane redistribution of the Escherichia coli MinD protein induced by MinE. J Bacteriol. 2000; 182(3):613-9. PMC: 94322. DOI: 10.1128/JB.182.3.613-619.2000. View

King G, Shih Y, Maciejewski M, Bains N, Pan B, Rowland S . Structural basis for the topological specificity function of MinE. Nat Struct Biol. 2000; 7(11):1013-7. DOI: 10.1038/80917. View

Fu X, Shih Y, Zhang Y, Rothfield L . The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle. Proc Natl Acad Sci U S A. 2001; 98(3):980-5. PMC: 14695. DOI: 10.1073/pnas.98.3.980. View

Hale C, Meinhardt H, de Boer P . Dynamic localization cycle of the cell division regulator MinE in Escherichia coli. EMBO J. 2001; 20(7):1563-72. PMC: 145461. DOI: 10.1093/emboj/20.7.1563. View

Hu Z, Lutkenhaus J . Topological regulation of cell division in E. coli. spatiotemporal oscillation of MinD requires stimulation of its ATPase by MinE and phospholipid. Mol Cell. 2001; 7(6):1337-43. DOI: 10.1016/s1097-2765(01)00273-8. View

Rothfield L, Shih Y, King G . Polar explorers: membrane proteins that determine division site placement. Cell. 2001; 106(1):13-6. DOI: 10.1016/s0092-8674(01)00432-9. View

Hu Z, Gogol E, Lutkenhaus J . Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE. Proc Natl Acad Sci U S A. 2002; 99(10):6761-6. PMC: 124476. DOI: 10.1073/pnas.102059099. View

10.

Shih Y, Fu X, King G, Le T, Rothfield L . 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 J. 2002; 21(13):3347-57. PMC: 126078. DOI: 10.1093/emboj/cdf323. View

11.

Hu Z, Saez C, Lutkenhaus J . Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE. J Bacteriol. 2002; 185(1):196-203. PMC: 141945. DOI: 10.1128/JB.185.1.196-203.2003. View

12.

Suefuji K, Valluzzi R, Raychaudhuri D . Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE. Proc Natl Acad Sci U S A. 2002; 99(26):16776-81. PMC: 139220. DOI: 10.1073/pnas.262671699. View

13.

Lackner L, Raskin D, de Boer P . ATP-dependent interactions between Escherichia coli Min proteins and the phospholipid membrane in vitro. J Bacteriol. 2003; 185(3):735-49. PMC: 142821. DOI: 10.1128/JB.185.3.735-749.2003. View

14.

Ishidate K, Creeger E, Zrike J, Deb S, Glauner B, Macalister T . Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membranes and the murein skeleton of the cell envelope. J Biol Chem. 1986; 261(1):428-43. View

15.

de Boer P, Crossley R, Rothfield L . A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli. Cell. 1989; 56(4):641-9. DOI: 10.1016/0092-8674(89)90586-2. View

16.

Zhao C, de Boer P, Rothfield L . Proper placement of the Escherichia coli division site requires two functions that are associated with different domains of the MinE protein. Proc Natl Acad Sci U S A. 1995; 92(10):4313-7. PMC: 41934. DOI: 10.1073/pnas.92.10.4313. View

17.

Pichoff S, Vollrath B, Touriol C, Bouche J . Deletion analysis of gene minE which encodes the topological specificity factor of cell division in Escherichia coli. Mol Microbiol. 1995; 18(2):321-9. DOI: 10.1111/j.1365-2958.1995.mmi_18020321.x. View

18.

Huang J, Cao C, Lutkenhaus J . Interaction between FtsZ and inhibitors of cell division. J Bacteriol. 1996; 178(17):5080-5. PMC: 178301. DOI: 10.1128/jb.178.17.5080-5085.1996. View

19.

Raskin D, de Boer P . The MinE ring: an FtsZ-independent cell structure required for selection of the correct division site in E. coli. Cell. 1997; 91(5):685-94. DOI: 10.1016/s0092-8674(00)80455-9. View

20.

Zhang Y, Rowland S, King G, Braswell E, Rothfield L . The relationship between hetero-oligomer formation and function of the topological specificity domain of the Escherichia coli MinE protein. Mol Microbiol. 1998; 30(2):265-73. DOI: 10.1046/j.1365-2958.1998.01059.x. View