RNA-protein interactions in 30S ribosomal subunits: Folding and function of 16S rRNA

Seth Stern, Ted Powers, L. I Ming Changchien, Harry F. Noller

Research output: Contribution to journalArticle

209 Scopus citations

Abstract

Chemical probing methods have been used to "footprint" 165 ribosomal RNA (rRNA) at each step during the in vitro assembly of twenty 30S subunit ribosomal proteins. These experiments yield information about the location of each protein relative to the structure of 16S rRNA and provide the basis for derivation of a detailed model for the three-dimensional folding of 16S rRNA. Several lines of evidence suggest that protein-dependent conformational changes in 16S rRNA play an important part in the cooperativity of ribosome assembly and in fine-tuning of the conformation and dynamics of 16S rRNA in the 30S subunit.

Original languageEnglish (US)
Pages (from-to)783-790
Number of pages8
JournalScience
Volume244
Issue number4906
StatePublished - 1989

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'RNA-protein interactions in 30S ribosomal subunits: Folding and function of 16S rRNA'. Together they form a unique fingerprint.

  • Cite this

    Stern, S., Powers, T., Changchien, L. I. M., & Noller, H. F. (1989). RNA-protein interactions in 30S ribosomal subunits: Folding and function of 16S rRNA. Science, 244(4906), 783-790.