2M6P
The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase
Summary for 2M6P
| Entry DOI | 10.2210/pdb2m6p/pdb |
| Related | 2M6O |
| NMR Information | BMRB: 19149 |
| Descriptor | uncharacterized protein Mb2076 (1 entity in total) |
| Functional Keywords | mv2050, mtb, rnap, sigma factor, transcription |
| Biological source | Mycobacterium bovis |
| Total number of polymer chains | 1 |
| Total formula weight | 5213.68 |
| Authors | Liu, B.,Parsy, M.,Paget, M.,Matthews, S. (deposition date: 2013-04-06, release date: 2013-05-08, Last modification date: 2024-05-01) |
| Primary citation | Tabib-Salazar, A.,Liu, B.,Doughty, P.,Lewis, R.A.,Ghosh, S.,Parsy, M.L.,Simpson, P.J.,O'Dwyer, K.,Matthews, S.J.,Paget, M.S. The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase. Nucleic Acids Res., 41:5679-5691, 2013 Cited by PubMed Abstract: RbpA 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 σ subunit in these organisms, but not to more diverged alternative σ 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-σ interaction is mediated by the C-terminal region of RbpA and σ domain 2, and S. coelicolor RbpA mutants that are defective in binding σ 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 σ cycle in actinobacteria. PubMed: 23605043DOI: 10.1093/nar/gkt277 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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