Analysis of conformational changes in 16 S rRNA during the course of 30 S subunit assembly

Kristi L. Holmes, Gloria M. Culver*

*Corresponding author for this work

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

Ribosome biogenesis involves an integrated series of binding events coupled with conformational changes that ultimately result in the formation of a functional macromolecular complex. In vitro, Escherichia coli 30 S subunit assembly occurs in a cooperative manner with the ordered addition of 20 ribosomal proteins (r-proteins) with 16 S rRNA. The assembly pathway for 30 S subunits has been dissected in vitro into three steps, where specific r-proteins associate with 16 S rRNA early in 30 S subunit assembly, followed by a mid-assembly conformational rearrangement of the complex that then enables the remaining r-proteins to associate in the final step. Although the three steps of 30 S subunit assembly have been known for some time, few details have been elucidated about changes that occur as a result of these three specific stages. Here, we present a detailed analysis of the concerted early and late stages of small ribosomal subunit assembly. Conformational changes, roles for base-pairing and r-proteins at specific stages of assembly, and a polar nature to the assembly process have been revealed. This work has allowed a more comprehensive and global view of E. coli 30 S ribosomal subunit assembly to be obtained.

Original languageEnglish (US)
Pages (from-to)340-357
Number of pages18
JournalJournal of Molecular Biology
Volume354
Issue number2
DOIs
StatePublished - Nov 25 2005

Keywords

  • 16 S rRNA
  • 30 S subunit
  • Conformational change
  • Ribosomal protein
  • Ribosome

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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