Barnase and barstar: two small proteins to fold and fit together

Trends Biochem Sci. 1989 Nov;14(11):450-4. doi: 10.1016/0968-0004(89)90104-7.

Abstract

Barnase and barstar are the extracellular ribonuclease and its intracellular inhibitor produced by Bacillus amyloliquefaciens. Both are small single-chain proteins and thus are suitable for application to the study of how a protein's sequence directs its fold. Barnase has neither disulfide bonds nor non-peptide components and unfolds reversibly in what closely approximates a two-state reaction. The genes for both these proteins have been cloned in E. coli. Expression of barstar is necessary to counter the lethal effect of expressed active barnase. Site-directed mutagenesis is being used to answer specific and general questions relating to protein folding and protein-protein interaction.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacillus / enzymology*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cloning, Molecular
  • Genes, Bacterial
  • Molecular Sequence Data
  • Protein Conformation
  • Ribonucleases / antagonists & inhibitors
  • Ribonucleases / genetics
  • Ribonucleases / metabolism*

Substances

  • Bacterial Proteins
  • barstar protein, Bacillus amyloliquefaciens
  • Ribonucleases
  • Bacillus amyloliquefaciens ribonuclease