Ribosomal protein L4 of Escherichia coli: in vitro analysis of L4-mediated attenuation control

Biochimie. 1991 Jun;73(6):719-27. doi: 10.1016/0300-9084(91)90052-3.

Abstract

Ribosomal protein L4 of Escherichia coli functions not only as a component of the ribosome but also as a regulatory factor inhibiting both transcription and translation of its own operon, the 11 gene S10 operon. L4-mediated transcription control results in premature termination of transcription within the 172 base S10 operon leader. This attenuation control can be reproduced in a purified transcription system containing RNA polymerase, but depends on the addition of transcription factor NusA. The NusA stimulation saturates at about 2-4 copies per RNA polymerase. The L4 effect plateaus at about 4 copies per RNA polymerase. The specific recognition sites on 23S rRNA and in the S10 leader for L4 binding are not yet known. However, we can demonstrate that a fragment of 23S rRNA containing the proximal 840 bases can eliminate in vitro L4-stimulated attenuation, and hence, contains the information sufficient for L4 binding to 23S rRNA.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Base Sequence
  • Binding Sites
  • DNA Mutational Analysis
  • DNA-Directed RNA Polymerases / metabolism
  • Escherichia coli / metabolism*
  • Gene Expression Regulation, Bacterial*
  • In Vitro Techniques
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Operon / genetics*
  • RNA, Ribosomal, 16S / metabolism
  • RNA, Ribosomal, 23S / chemistry*
  • Ribosomal Proteins / metabolism*
  • Transcription, Genetic*

Substances

  • RNA, Ribosomal, 16S
  • RNA, Ribosomal, 23S
  • Ribosomal Proteins
  • ribosomal protein L4
  • DNA-Directed RNA Polymerases