Monobesh Patra

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In the standard method of transformation of Escherichia coli with extraneous DNA, cells are made competent for DNA uptake by incubating in ice-cold 100 mM CaCl(2). Analysis of the whole protein profile of CaCl(2)-treated E. coli cells by the techniques of one- and two-dimensional gel electrophoresis, MALDI-MS and immunoprecipitation revealed overproduction(More)
Heat-stress to any living cell is known to trigger a universal defense response, called heat-shock response, with rapid induction of tens of different heat-shock proteins. Bacterial heat-shock genes are transcribed by the σ(32)-bound RNA polymerase instead of the normal σ(70)-bound RNA polymerase. In this study, the diversity in sequence, variation in(More)
The stability of heat-shock transcription factor σ(32) in Escherichia coli has long been known to be modulated only by its own transcribed chaperone DnaK. Very few reports suggest a role for another heat-shock chaperone, GroEL, for maintenance of cellular σ(32) level. The present study demonstrates in vivo physical association between GroEL and σ(32) in E.(More)
E. coli small heat shock proteins IbpA and IbpB (inclusion body binding proteins A and B) are known to act as holding chaperones on denaturing, aggregate-prone proteins. But, there is no clear understanding about which of the IbpA and IbpB has more holdase activity and how the holdase activity of one was influenced by the presence of the other. This study(More)
The heat shock response mechanism is a very vital biochemical process and is mainly controlled by σ(32) protein. The function of σ(32) is temperature dependent and at lower temperatures σ(32) is inactivated by its interactions with DnaK. This interaction is completely abolished above 42°C till date no molecular details of the interactions are available. In(More)
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