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Inter-subunit recognition and manifestation of segmental mobility in Escherichia coli RNA polymerase: a case study with ω–β′ interaction by Pallavi Ghosh; Chandrashekharan Ramakrishnan; Dipankar Chatterji is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Omega (omega), consisting of 91 amino acids, is the smallest of all the Escherichia coli RNA polymerase subunits and is organized into an N-terminal domain of 53 amino acids followed by an unstructured tail in the C-terminal region. Our earlier experiments have shown a chaperone-like function of omega in which it helps to maintain beta' in a correct conformation and recruit it to the alpha(2)beta subassembly to form a functional core enzyme (alpha(2)betabeta'omega). The X-ray structure analysis of Thermus aquaticus core RNA polymerase suggests that two regions of omega latch onto the N-terminal and C-terminal ends of the beta'-subunit. In the present study we have monitored the conformational changes in beta' as the denatured protein is refolded in the presence and absence of omega using tryptophan fluorescence emission of beta' as well as acrylamide quenching of Trp fluorescence. Results indicate that the presence of stoichiometric amounts of omega is helpful in beta' refolding. We have also monitored the behavior of the C-terminal tail of omega by engineering three cysteine residues at three different sites in omega and subsequently labeling them with a sulphydryl-specific fluore

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Author

Pallavi Ghosh; Chandrashekharan Ramakrishnan; Dipankar Chatterji

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0301-4622)

Published

2003

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)