Please use this identifier to cite or link to this item:
|Title:||Mycobacterium tuberculosis RNA Polymerase-binding Protein A (RbpA) and Its Interactions with Sigma Factors|
Muskett, Frederick W.
Waters, Lorna C.
Addis, Philip W.
Carr, Mark D.
O'Hare, Helen M.
|Publisher:||American Society for Biochemistry and Molecular Biology|
|Citation:||The Journal of Biological Chemistry, 2013, 288 (20), pp. 14438-14450|
|Abstract:||RNA polymerase-binding protein A (RbpA), encoded by Rv2050, is specific to the actinomycetes, where it is highly conserved. In the pathogen Mycobacterium tuberculosis, RbpA is essential for growth and survival. RbpA binds to the β subunit of the RNA polymerase where it activates transcription by unknown mechanisms, and it may also influence the response of M. tuberculosis to the current frontline anti-tuberculosis drug rifampicin. Here we report the solution structure of RbpA and identify the principle sigma factor σ[superscript A] and the stress-induced σ[superscript B] as interaction partners. The protein has a central ordered domain with a conserved hydrophobic surface that may be a potential protein interaction site. The N and C termini are highly dynamic and are involved in the interaction with the sigma factors. RbpA forms a tight complex with the N-terminal domain of σB via its N- and C-terminal regions. The interaction with sigma factors may explain how RbpA stabilizes sigma subunit binding to the core RNA polymerase and thereby promotes initiation complex formation. RbpA could therefore influence the competition between principal and alternative sigma factors and hence the transcription profile of the cell.|
|Rights:||Copyright © 2013, American Society for Biochemistry and Molecular Biology. Deposited with reference to the publisher’s archiving policy available on the SHERPA/RoMEO website.|
|Description:||This research was originally published in The Journal of Biological Chemistry. Bortoluzzi, A., Muskett, F.W. et al., Mycobacterium tuberculosis RNA Polymerase-binding Protein A (RbpA) and Its Interactions with Sigma Factors, The Journal of Biological Chemistry, 2013, 288 (20), pp. 14438-14450, © the American Society for Biochemistry and Molecular Biology.|
|Appears in Collections:||Published Articles, Dept. of Infection, Immunity and Inflammation|
Files in This Item:
|RbpA manuscript revision March27.pdf||Post-review (final submitted)||5.94 MB||Adobe PDF||View/Open|
Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.