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
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Creator |
SINGH, P
MAKDE, RD GHOSH, S ASTHANA, J KUMAR, V PANDA, D |
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Subject |
Bacterial cytokinesis
FtsA Protein assembly Bis-ANS ATPase CELL-DIVISION PROTEIN ACTIN-LIKE FTSA ESCHERICHIA-COLI Z-RING DYNAMICS BINDING ZIPA PROTOFILAMENTS MEMBRANE |
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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.
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Publisher |
ELSEVIER SCIENCE BV
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Date |
2014-10-15T08:04:53Z
2014-10-15T08:04:53Z 2013 |
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Type |
Article
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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 |
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Language |
en
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