The long-range goal of this project is to determine the mechanism used by bacteria to select the proper cell division site at midcell. The three Min proteins, MinC, MinD and MinE, are required for proper site selection. The proteins have a unique cellular localization pattern and undergo a unique pole-to-pole oscillatory cycle. We have recently shown that the MinCDE proteins are organized into spiral filaments that wind around the cell between the two poles in a cytoskeletal-like structure that appears distinct from a coiled structure formed by the MreB protein. During the proposed grant period we will use a combination of fluorescence microscopy, biochemistrry and genetics to achieve the following aims: i. Min protein structure and function-- To determine the effects of mutations that interfere with the topological specificity function of the MinCDE system, ii. Long-range organization of the Min system-- To define the organization of the MinDE cytoskeletal-like elements within the cell, to determine whether the Min and MreB spiral filaments are separate structures, to characterize proteins that interact with MinD and MinE, and to determine whether there is a relationship between the Min spiral filaments and chromosome segregation, iii. MreB-- To isolate the MreB and Min cytoskeletal-like structures, to characterize proteins that interact with MreB, and to define the behavior of the MreB cytoskeletal-like structures during the course of the cell cycle.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
5R37GM060632-14
Application #
8451410
Study Section
Special Emphasis Panel (NSS)
Program Officer
Deatherage, James F
Project Start
2000-02-01
Project End
2014-03-31
Budget Start
2013-04-01
Budget End
2014-03-31
Support Year
14
Fiscal Year
2013
Total Cost
$483,424
Indirect Cost
$169,512
Name
University of Connecticut
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
022254226
City
Farmington
State
CT
Country
United States
Zip Code
06030
Taghbalout, Aziz; Yang, Qingfen; Arluison, Veronique (2014) The Escherichia coli RNA processing and degradation machinery is compartmentalized within an organized cellular network. Biochem J 458:11-22
Lu, Feng; Taghbalout, Aziz (2013) Membrane association via an amino-terminal amphipathic helix is required for the cellular organization and function of RNase II. J Biol Chem 288:7241-51
Taghbalout, Aziz; Yang, Qingfen (2010) Self-assembly of the bacterial cytoskeleton-associated RNA helicase B protein into polymeric filamentous structures. J Bacteriol 192:3222-6
Taghbalout, Aziz; Ma, Luyan; Rothfield, Lawrence (2006) Role of MinD-membrane association in Min protein interactions. J Bacteriol 188:2993-3001
Drew, Donald A; Osborn, Mary J; Rothfield, Lawrence I (2005) A polymerization-depolymerization model that accurately generates the self-sustained oscillatory system involved in bacterial division site placement. Proc Natl Acad Sci U S A 102:6114-8
Shih, Yu-Ling; Kawagishi, Ikuro; Rothfield, Lawrence (2005) The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation. Mol Microbiol 58:917-28
Ma, Luyan; King, Glenn F; Rothfield, Lawrence (2004) Positioning of the MinE binding site on the MinD surface suggests a plausible mechanism for activation of the Escherichia coli MinD ATPase during division site selection. Mol Microbiol 54:99-108
Ma, Lu-Yan; King, Glenn; Rothfield, Lawrence (2003) Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli. J Bacteriol 185:4948-55
Shih, Yu-Ling; Le, Trung; Rothfield, Lawrence (2003) Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc Natl Acad Sci U S A 100:7865-70
Shih, Yu-Ling; Fu, Xiaoli; King, Glenn F et al. (2002) 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 21:3347-57

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