TY - JOUR
AB - <p>Transcription termination is an essential step in transcription by RNA polymerase (RNAP) and crucial for gene regulation. For many bacterial genes, transcription termination is mediated by the ATP-dependent RNA translocase/helicase Rho, which causes the dissociation of RNA/DNA from RNAP elongation complex (EC). However, structural basis of the interplay between Rho and RNAP remains obscure. Here we report the cryo-electron microscopy structure of the Rho-engaged EC. The Rho hexamer binds RNAP through the C-terminal domains, which surround the RNA-exit site of RNAP, directing the nascent RNA seamlessly from the RNA exit to the Rho central channel. The b-flap tip at the RNA exit is critical to the Rho-dependent RNA release, and its deletion causes an alternative Rho-RNAP binding mode, which is irrelevant to termination. The Rho-binding site overlaps with the binding sites of other macromolecules, such as ribosomes, providing a general basis of gene regulation.</p>
TI - Structural basis of the transcription termination factor Rho engagement with transcribing RNA polymerase
JF - bioRxiv
DO - 10.1101/2022.09.02.506315
DA - 2022-09-03
UR - https://www.deepdyve.com/lp/biorxiv/structural-basis-of-the-transcription-termination-factor-rho-Lu5VrFzR0k
SP - 2022.09.02.506315
DP - DeepDyve
ER -