Cloning, characterization and expression of the polypeptide release factor gene, eRF1, of Blepharisma japonicum

Biotechnol Lett. 2004 Jun;26(12):959-63. doi: 10.1023/b:bile.0000030039.42124.36.

Abstract

The polypeptide release factor gene, eRF1, of Blepharisma japonicum (Bj-eRF1) was cloned and sequenced. Its coding region was 1314 base pairs and encodes a protein of 437 amino acids. The cloned gene was expressed in Escherichia coli and the recombinant Bj-eRF1 polypeptide was purified by Ni2+-nitrilotriacetic acid agarose and Superose12 chromatography. Pull-down analysis showed that the recombinant Bj-eRF1 interacts with the heterologously-expressed release factor, eRF3C, of Euplotes octocarinatus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cloning, Molecular / methods
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism*
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Termination Factors / biosynthesis*
  • Peptide Termination Factors / chemistry
  • Peptide Termination Factors / genetics*
  • Protein Binding
  • Protein Engineering / methods*
  • Protozoan Proteins / biosynthesis*
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Spiroplasma / genetics*
  • Spiroplasma / metabolism*
  • Transformation, Bacterial / genetics

Substances

  • Peptide Termination Factors
  • Protozoan Proteins
  • Recombinant Proteins
  • peptide-chain-release factor 3