Transcription complexes as RNA chaperones

Transcription. 2021 Aug;12(4):126-155. doi: 10.1080/21541264.2021.1985931. Epub 2021 Nov 1.

Abstract

To exert their functions, RNAs adopt diverse structures, ranging from simple secondary to complex tertiary and quaternary folds. In vivo, RNA folding starts with RNA transcription, and a wide variety of processes are coupled to co-transcriptional RNA folding events, including the regulation of fundamental transcription dynamics, gene regulation by mechanisms like attenuation, RNA processing or ribonucleoprotein particle formation. While co-transcriptional RNA folding and associated co-transcriptional processes are by now well accepted as pervasive regulatory principles in all organisms, investigations into the role of the transcription machinery in co-transcriptional folding processes have so far largely focused on effects of the order in which RNA regions are produced and of transcription kinetics. Recent structural and structure-guided functional analyses of bacterial transcription complexes increasingly point to an additional role of RNA polymerase and associated transcription factors in supporting co-transcriptional RNA folding by fostering or preventing strategic contacts to the nascent transcripts. In general, the results support the view that transcription complexes can act as RNA chaperones, a function that has been suggested over 30 years ago. Here, we discuss transcription complexes as RNA chaperones based on recent examples from bacterial transcription.

Keywords: Co-transcriptional RNA folding; RNA chaperone; cryoEM; single-molecule fluorescence; transcription factor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA-Directed RNA Polymerases / genetics
  • Nucleic Acid Conformation
  • RNA Folding*
  • RNA Processing, Post-Transcriptional
  • RNA* / chemistry
  • RNA* / genetics
  • Transcription, Genetic

Substances

  • RNA
  • DNA-Directed RNA Polymerases

Grants and funding

This work was supported by the Deutsche Forschungsgemeinschaft [WA 1126/11-1]; Deutsche Forschungsgemeinschaft [GRK 2473-1]; Deutsche Forschungsgemeinschaft [INST 130/1064-1]; Bundesministerium für Bildung und Forschung [ICMR2019-016 to M.C.W.]; Berlin University Alliance [501_BIS-CryoFac].