Document Detail

Assembly of Bacillus subtilis FtsA: Effects of pH, ionic strength and nucleotides on FtsA assembly.
MedLine Citation:
PMID:  23036588     Owner:  NLM     Status:  Publisher    
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'-disulphonic acid, inhibited the assembly of FtsA.
Parminder Singh; Ravindra D Makde; Saikat Ghosh; Jayant Asthana; Vinay Kumar; Dulal Panda
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-1
Journal Detail:
Title:  International journal of biological macromolecules     Volume:  -     ISSN:  1879-0003     ISO Abbreviation:  Int. J. Biol. Macromol.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-5     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7909578     Medline TA:  Int J Biol Macromol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier B.V.
Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India.
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