The long-range objective of this project is to understand the mechanism used by bacterial cells to place the division site at its proper location within the cell. To approach this goal, the bacterial minicell locus (minB) will be studied since mutation of this locus results in aberrant placement of the division septum. The studies are based on recent work showing that the miniB locus codes for several genes that affect the division process. The studies will use a combination of genetics, biochemistry and immunoelectronmicroscopy to localize the minB gene products within the cell, to identify their interactions with each other and with other protein components of the cell division machinery, to probe for possible enzymatic functions of one of the proteins, and to examine the interaction of the minB system with another gene product (dicB) whose effect on the cell division process is likely to be mediated by the minB system.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM041978-03
Application #
3300500
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1989-04-01
Project End
1992-03-31
Budget Start
1991-04-01
Budget End
1992-03-31
Support Year
3
Fiscal Year
1991
Total Cost
Indirect Cost
Name
University of Connecticut
Department
Type
Schools of Dentistry
DUNS #
City
Farmington
State
CT
Country
United States
Zip Code
06030
Fu, X; Shih, Y L; Zhang, Y et al. (2001) 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 98:980-5
Justice, S S; Garcia-Lara, J; Rothfield, L I (2000) Cell division inhibitors SulA and MinC/MinD block septum formation at different steps in the assembly of the Escherichia coli division machinery. Mol Microbiol 37:410-23
Rowland, S L; Fu, X; Sayed, M A et al. (2000) Membrane redistribution of the Escherichia coli MinD protein induced by MinE. J Bacteriol 182:613-9
King, G F; Rowland, S L; Pan, B et al. (1999) The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain. Mol Microbiol 31:1161-9
King, G F; Pan, B; Maciejewski, M W et al. (1999) Backbone and side-chain 1H, 15N, and 13C assignments for the topological specificity domain of the MinE cell division protein. J Biomol NMR 13:395-6
Zhang, Y; Rowland, S; King, G et al. (1998) The relationship between hetero-oligomer formation and function of the topological specificity domain of the Escherichia coli MinE protein. Mol Microbiol 30:265-73
Zhao, C R; de Boer, P A; Rothfield, L I (1995) 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 92:4313-7
Wang, X D; de Boer, P A; Rothfield, L I (1991) A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli. EMBO J 10:3363-72