Nucl._Acids_Res.-2013-Tabib-Salazar-5679-91.pdf (3.16 MB)
The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase
journal contribution
posted on 2023-06-08, 14:49 authored by Aline Tabib-Salazar, Bing Liu, Philip Doughty, Richard A Lewis, Somadri Ghosh, Marie-Laure Parsy, Peter J Simpson, Kathleen O'Dwyer, Steve J Matthews, Mark PagetMark PagetRbpA is a small non-DNA-binding transcription factor that associates with RNA polymerase holoenzyme and stimulates transcription in actinobacteria, including Streptomyces coelicolor and Mycobacterium tuberculosis. RbpA seems to show specificity for the vegetative form of RNA polymerase as opposed to alternative forms of the enzyme. Here, we explain the basis of this specificity by showing that RbpA binds directly to the principal s subunit in these organisms, but not to more diverged alternative s factors. Nuclear magnetic resonance spectroscopy revealed that, although differing in their requirement for structural zinc, the RbpA orthologues from S. coelicolor and M. tuberculosis share a common structural core domain, with extensive, apparently disordered, N- and C-terminal regions. The RbpA-s interaction is mediated by the C-terminal region of RbpA and s domain 2, and S. coelicolor RbpA mutants that are defective in binding s are unable to stimulate transcription in vitro and are inactive in vivo. Given that RbpA is essential in M. tuberculosis and critical for growth in S. coelicolor, these data support a model in which RbpA plays a key role in the s cycle in actinobacteria.
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Publication status
- Published
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- Published version
Journal
Nucleic Acids ResearchISSN
0305-1048Publisher
Oxford University PressExternal DOI
Issue
11Volume
41Page range
5679-5691Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2013-04-29First Open Access (FOA) Date
2016-03-22First Compliant Deposit (FCD) Date
2016-11-16Usage metrics
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