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Assembly of Bacillus subtilis FtsA: Effects of pH, ionic strength and nucleotides on FtsA assembly

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Title Assembly of Bacillus subtilis FtsA: Effects of pH, ionic strength and nucleotides on FtsA assembly
 
Creator SINGH, P
MAKDE, RD
GHOSH, S
ASTHANA, J
KUMAR, V
PANDA, D
 
Subject Bacterial cytokinesis
FtsA
Protein assembly
Bis-ANS
ATPase
CELL-DIVISION PROTEIN
ACTIN-LIKE FTSA
ESCHERICHIA-COLI
Z-RING
DYNAMICS
BINDING
ZIPA
PROTOFILAMENTS
MEMBRANE
 
Description In this work, the assembly of purified Bacillus subtilis FtsA was analyzed by several complimentary techniques. FtsA assembled to form filaments and bundles and the polymers disassembled upon dilution. FtsA assembled more efficiently at pH 6.0 as compared to that at pH 7.0 or 8.0 and high salt inhibited the assembly of FtsA. FtsA was found to hydrolyze ATP in vitro; however, neither ATP nor ADP influenced the assembly kinetics of FtsA. Though FtsA is a homologue of actin, cytochalasin D did not inhibit the assembly of FtsA. Interestingly, a hydrophobic molecule, 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid, inhibited the assembly of FtsA. (c) 2012 Elsevier B.V. All rights reserved.
 
Publisher ELSEVIER SCIENCE BV
 
Date 2014-10-15T08:04:53Z
2014-10-15T08:04:53Z
2013
 
Type Article
 
Identifier INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 52170-176
http://dx.doi.org/10.1016/j.ijbiomac.2012.09.019
http://dspace.library.iitb.ac.in/jspui/handle/100/14637
 
Language en