Direct interaction between two Escherichia coli transcription antitermination factors, NusB and ribosomal protein S10

J Mol Biol. 1992 Jan 5;223(1):55-66. doi: 10.1016/0022-2836(92)90715-v.

Abstract

The Escherichia coli proteins NusB and ribosomal protein S10 are important for transcription antitermination by the bacteriophage lambda N protein. We have used sucrose gradient co-sedimentation and affinity chromatography with immobilized ribosomal protein S10, a glutathione S-transferase-S10 fusion protein, and NusB to show that NusB binds directly and very selectively to S10. The interaction is non-ionic and has an estimated Kd value of 10(-7) M. We hypothesize that NusB binds to N-modified transcription complexes primarily by interacting with S10.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics*
  • Chromatography, Affinity
  • Escherichia coli / genetics*
  • Escherichia coli Proteins*
  • Gene Expression Regulation, Bacterial*
  • Mutation
  • Protein Binding
  • Recombinant Fusion Proteins / metabolism
  • Ribosomal Proteins / genetics*
  • Terminator Regions, Genetic*
  • Transcription Factors
  • Transcription, Genetic*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • NusB protein, E coli
  • Recombinant Fusion Proteins
  • Ribosomal Proteins
  • Transcription Factors
  • ribosomal protein S10