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GTP Regulates the Interaction between MciZ and FtsZ: A Possible Role of MciZ in Bacterial Cell Division

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Title GTP Regulates the Interaction between MciZ and FtsZ: A Possible Role of MciZ in Bacterial Cell Division
 
Creator RAY, S
KUMAR, A
PANDA, D
 
Subject C-TERMINAL TAIL
PROTEIN FTSZ
ESCHERICHIA-COLI
ASSEMBLY DYNAMICS
BACILLUS-SUBTILIS
GUANINE-NUCLEOTIDES
CYTOKINESIS
BINDING
CYTOSKELETON
PROTOFILAMENTS
 
Description MciZ, a peptide with 40 amino acid residues, has been shown to be expressed during bacterial sporulation, to inhibit Z-ring formation in bacteria, and to inhibit the assembly of FtsZ in vitro. Here, MciZ was found to bind to FtsZ in vitro with a dissociation constant of 0.3 +/- 0.1 mu M. Guanosine nucleotides inhibited the binding of MciZ to FtsZ; however, GTP inhibited the binding of MciZ to FtsZ more strongly than GDP. In addition, MciZ inhibited the binding of 2',3'-O-(2,4,6-trinitrocyclohexadienylidene)-GTP, a fluorescent analogue of GTP, to FtsZ. The results indicated that MciZ shares its binding site on FtsZ with GTP. Furthermore, M19I, an N-terminal 19-residue peptide (MKVHRMPKGVVLVGKAWEI) of MciZ, inhibited the assembly and GTPase activity of FtsZ in vitro. The results suggested that GTP plays an important role in the regulation of the interaction between FtsZ and MciZ and that M19I may be used as a lead peptide to design peptide inhibitors of FtsZ assembly.
 
Publisher AMER CHEMICAL SOC
 
Date 2014-10-15T11:50:03Z
2014-10-15T11:50:03Z
2013
 
Type Article
 
Identifier BIOCHEMISTRY, 52(2)392-401
http://dx.doi.org/10.1021/bi301237m
http://dspace.library.iitb.ac.in/jspui/handle/100/14830
 
Language en