RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli

Katharina Semrad, Rachel Green, Renée Schroeder

Research output: Contribution to journalArticlepeer-review

Abstract

The ribosome is a highly dynamic ribonucleoprotein machine. During assembly and during translation the ribosomal RNAs must routinely be prevented from falling into kinetic folding traps. Stable occupation of these trapped states may be prevented by proteins with RNA chaperone activity. Here, ribosomal proteins from the large (50S) ribosome subunit of Escherichia coli were tested for RNA chaperone activity in an in vitro trans splicing assay. Nearly a third of the 34 large ribosomal subunit proteins displayed RNA chaperone activity. We discuss a possible role of this function during ribosome assembly and during translation.

Original languageEnglish (US)
Pages (from-to)1855-1860
Number of pages6
JournalRNA
Volume10
Issue number12
DOIs
StatePublished - Dec 2004

Keywords

  • 50S subunit
  • RNA chaperone
  • RNA folding
  • Ribosomal proteins
  • trans splicing

ASJC Scopus subject areas

  • Molecular Biology

Fingerprint

Dive into the research topics of 'RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli'. Together they form a unique fingerprint.

Cite this