Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM029764-16
Application #
2175615
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1981-07-01
Project End
2000-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
16
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Kansas
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
016060860
City
Kansas City
State
KS
Country
United States
Zip Code
66160
Park, Kyung-Tae; Dajkovic, Alex; Wissel, Mark et al. (2018) MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z ring disassembly. J Biol Chem 293:5834-5846
Du, Shishen; Pichoff, Sebastien; Kruse, Karsten et al. (2018) FtsZ filaments have the opposite kinetic polarity of microtubules. Proc Natl Acad Sci U S A 115:10768-10773
Du, Shishen; Lutkenhaus, Joe (2017) Assembly and activation of the Escherichia coli divisome. Mol Microbiol 105:177-187
Park, Kyung-Tae; Villar, Maria T; Artigues, Antonio et al. (2017) MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation. Proc Natl Acad Sci U S A 114:7497-7504
Du, Shishen; Lutkenhaus, Joe (2017) The N-succinyl-l,l-diaminopimelic acid desuccinylase DapE acts through ZapB to promote septum formation in Escherichia coli. Mol Microbiol 105:326-345
Du, Shishen; Pichoff, Sebastien; Lutkenhaus, Joe (2016) FtsEX acts on FtsA to regulate divisome assembly and activity. Proc Natl Acad Sci U S A 113:E5052-61
Du, Shishen; Park, Kyung-Tae; Lutkenhaus, Joe (2015) Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA. Mol Microbiol 95:173-88
Park, Kyung-Tae; Du, Shishen; Lutkenhaus, Joe (2015) MinC/MinD copolymers are not required for Min function. Mol Microbiol 98:895-909
Pichoff, Sebastien; Du, Shishen; Lutkenhaus, Joe (2015) The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring. Mol Microbiol 95:971-87
Du, Shishen; Lutkenhaus, Joe (2014) SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD. PLoS Genet 10:e1004460

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