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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Cloning, Molecular / methods
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Escherichia coli / genetics*
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Escherichia coli / metabolism*
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Molecular Sequence Data
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Molecular Weight
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Peptide Termination Factors / biosynthesis*
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Peptide Termination Factors / chemistry
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Peptide Termination Factors / genetics*
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Protein Binding
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Protein Engineering / methods*
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Protozoan Proteins / biosynthesis*
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Protozoan Proteins / chemistry
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Protozoan Proteins / genetics*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Spiroplasma / genetics*
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Spiroplasma / metabolism*
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Transformation, Bacterial / genetics
Substances
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Peptide Termination Factors
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Protozoan Proteins
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Recombinant Proteins
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peptide-chain-release factor 3