title: Assembly of Bacillus subtilis FtsA: effects of pH, ionic strength and nucleotides on FtsA assembly.
abstract: 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.
authors.affiliation: Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India.
authors.forename: Parminder
authors.initials: P
authors.lastname: Singh
authors.forename: Ravindra D
authors.initials: RD
authors.lastname: Makde
authors.forename: Saikat
authors.initials: S
authors.lastname: Ghosh
authors.forename: Jayant
authors.initials: J
authors.lastname: Asthana
authors.forename: Vinay
authors.initials: V
authors.lastname: Kumar
authors.forename: Dulal
authors.initials: D
authors.lastname: Panda
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D001412:Bacillus subtilis / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D009705:Nucleosides / Q000737:chemistry* / Q000378:metabolism; D009994:Osmolar Concentration
chemical_list: D001426:Bacterial Proteins; C065103:FtsA protein, Bacteria; D009705:Nucleosides; D000255:Adenosine Triphosphate