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

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+-nitri...

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Veröffentlicht in:	Biotechnology letters 2004-06, Vol.26 (12), p.959-963
Hauptverfasser:	WEI WANG, CHAI, Bao-Feng, HECKMANN, Klaus, LIANG, Ai-Hua
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids Binding Sites Biological and medical sciences Biotechnology Blepharisma japonicum Cloning Cloning, Molecular - methods E coli Escherichia coli - genetics Escherichia coli - metabolism Euplotes octocarinatus Fundamental and applied biological sciences. Psychology Gel chromatography Genes Molecular Sequence Data Molecular Weight Nitrilotriacetic acid Peptide Termination Factors - biosynthesis Peptide Termination Factors - chemistry Peptide Termination Factors - genetics Polypeptides Protein Binding Protein Engineering - methods Protozoan Proteins - biosynthesis Protozoan Proteins - chemistry Protozoan Proteins - genetics Q1 Q2 Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Spiroplasma - genetics Spiroplasma - metabolism Transformation, Bacterial - genetics
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Zusammenfassung:	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.
ISSN:	0141-5492 1573-6776
DOI:	10.1023/B:BILE.0000030039.42124.36