4WQS

Thermus thermophilus RNA polymerase backtracked complex

Summary for 4WQS

• Entry DOI: 10.2210/pdb4wqs/pdb
• Related: 3AOH 3AOI 4WQT
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total)
• Functional Keywords: transcription, rna cleavage, transferase-dna-rna complex, transferase/dna/rna
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 16
• Total formula weight: 796834.50

Authors

Murayama, Y.,Sekine, S.,Yokoyama, S. (deposition date: 2014-10-22, release date: 2015-02-18, Last modification date: 2024-03-20)

Primary citation

Sekine, S.I.,Murayama, Y.,Svetlov, V.,Nudler, E.,Yokoyama, S.
The Ratcheted and Ratchetable Structural States of RNA Polymerase Underlie Multiple Transcriptional Functions.
Mol.Cell, 57:408-421, 2015

PubMed Abstract: DNA-dependent RNA polymerase (RNAP) accomplishes multiple tasks during transcription by assuming different structural forms. Reportedly, the "tight" form performs nucleotide addition to nascent RNA, while the "ratcheted" form is adopted for transcription inhibition. In this study, we performed Cys-pair crosslinking (CPX) analyses of various transcription complexes of a bacterial RNAP and crystallographic analyses of its backtracked and Gre-factor-bound states to clarify which of the two forms is adopted. The ratcheted form was revealed to support GreA-dependent transcript cleavage, long backtracking, hairpin-dependent pausing, and termination. In contrast, the tight form correlated with nucleotide addition, mismatch-dependent pausing, one-nucleotide backtracking, and factor-independent transcript cleavage. RNAP in the paused/backtracked state, but not the nucleotide-addition state, readily transitions to the ratcheted form ("ratchetable"), indicating that the tight form represents two distinct regulatory states. The 3' end and the hairpin structure of the nascent RNA promote the ratchetable nature by modulating the trigger-loop conformation.

PubMed: 25601758
DOI: 10.1016/j.molcel.2014.12.014

Experimental method

X-RAY DIFFRACTION (4.306 Å)