Effect of protein binding on RNA folding

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Large RNA molecules are typically associated with proteins, some of which bind early to direct folding of the RNA and some of which bind later to maintain the correct RNA fold. Specifically how these proteins participate in the RNA folding process is not clear, but most appear to direct tertiary structure after the RNA has formed its secondary structure. CYT-18 binding to group I introns and S4 and S15 binding to 16S rRNA are examples of these interactions. DEAD box helicases unwind short duplexes in a folded RNA to allow it to rearrange its tertiary structure; examples are the helicase DbpA, which functions specifically on 23S rRNA, and Cyt-19 helicase, which works on many group I introns. What is known about these systems is related to what is generally understood about how proteins function to fold RNA.

Original languageEnglish
Title of host publicationComprehensive Biophysics
PublisherElsevier Inc.
Pages317-335
Number of pages19
Volume3
ISBN (Print)9780080957180
DOIs
StatePublished - Dec 1 2012

Keywords

  • 16S rRNA
  • CBP2
  • CYT-18
  • Cyt-19
  • DEAD box helicases
  • DbpA
  • Group I intron
  • Helix unwinding
  • RNA folding
  • RNA tertiary structure
  • Ribosomal protein S15
  • Ribosomal protein S4

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  • Cite this

    Hall, K. B. (2012). Effect of protein binding on RNA folding. In Comprehensive Biophysics (Vol. 3, pp. 317-335). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-374920-8.00326-X