2m6o

From Proteopedia
Revision as of 16:31, 22 February 2023 by OCA (talk | contribs)
Jump to navigation Jump to search

The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymeraseThe actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase

Structural highlights

2m6o is a 1 chain structure with sequence from Streptomyces coelicolor A3(2). Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RBPA_STRCO Binds to RNA polymerase (RNAP), stimulating transcription from principal, but not alternative sigma factor promoters. Stimulates transcription from several principal sigma factor HrdB (SigA)-dependent promoters but not from a SigR-dependent promoter. Stimulation occurs in the presence of the transcription initiation inhibitor rifampicin (Rif).[HAMAP-Rule:MF_01483][1] [2]

Publication Abstract from PubMed

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 sigma subunit in these organisms, but not to more diverged alternative sigma 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-sigma interaction is mediated by the C-terminal region of RbpA and sigma domain 2, and S. coelicolor RbpA mutants that are defective in binding sigma 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 sigma cycle in actinobacteria.

The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase.,Tabib-Salazar A, Liu B, Doughty P, Lewis RA, Ghosh S, Parsy ML, Simpson PJ, O'Dwyer K, Matthews SJ, Paget MS Nucleic Acids Res. 2013 Apr 19. PMID:23605043[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Newell KV, Thomas DP, Brekasis D, Paget MS. The RNA polymerase-binding protein RbpA confers basal levels of rifampicin resistance on Streptomyces coelicolor. Mol Microbiol. 2006 May;60(3):687-96. PMID:16629670 doi:10.1111/j.1365-2958.2006.05116.x
  2. Tabib-Salazar A, Liu B, Doughty P, Lewis RA, Ghosh S, Parsy ML, Simpson PJ, O'Dwyer K, Matthews SJ, Paget MS. The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase. Nucleic Acids Res. 2013 Apr 19. PMID:23605043 doi:10.1093/nar/gkt277
  3. Tabib-Salazar A, Liu B, Doughty P, Lewis RA, Ghosh S, Parsy ML, Simpson PJ, O'Dwyer K, Matthews SJ, Paget MS. The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase. Nucleic Acids Res. 2013 Apr 19. PMID:23605043 doi:10.1093/nar/gkt277
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA