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.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Method to Extend Research in Time (MERIT) Award (R37)
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Special Emphasis Panel (NSS)
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Deatherage, James F
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University of Connecticut
Schools of Medicine
United States
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Arluison, Véronique; Taghbalout, Aziz (2015) Cellular localization of RNA degradation and processing components in Escherichia coli. Methods Mol Biol 1259:87-101
Fortas, Emilie; Piccirilli, Federica; Malabirade, Antoine et al. (2015) New insight into the structure and function of Hfq C-terminus. Biosci Rep 35:
Cayrol, Bastien; Fortas, Emilie; Martret, Claire et al. (2015) Riboregulation of the bacterial actin-homolog MreB by DsrA small noncoding RNA. Integr Biol (Camb) 7:128-41
Taghbalout, Aziz; Yang, Qingfen; Arluison, Véronique (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 (2014) The Escherichia coli major exoribonuclease RNase II is a component of the RNA degradosome. Biosci Rep 34:e00166
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

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