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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Overexpression in Escherichia coli, Purification and Characterization of Thermoanaerobacter tengcongensis Elongation Factor G with Multiple Rare Codons

Author(s): Liqiang Zhang, Peng Xue and Hongjie Zhang

Volume 14, Issue 8, 2007

Page: [804 - 810] Pages: 7

DOI: 10.2174/092986607781483732

Price: $65


The fusA gene encoding a thermophilic protein EF-G with multiple rare condons was cloned from Thermoanaerobacter tengcongensis (TteEF-G) and overexpressed in Escherichia coli by cotransfering a RIG plasmid to overcome the potential codon-bias problem originated from Arg, Ile and Gly. The recombinant protein was identified by MALDITOF- MS for molecular mass with approximation of 76 kDa and by trypsin digestion coupled LC-MS/MS for peptide sequence coverage of 61.3%. The in vivo complementary assay indicates that TteEF-G could significantly rescue the E. coli LJ14 (frrts) at the non-permission temperature of 42°C in the bi-transformant of TteRRF and TteEF-G. This study indicated that coexpression of rare codons cognate tRNA is a useful method for protein overexpression in E. coli.

Keywords: Elongation factor G, RIG plasmid, gene expression, purification and characterization, Thermoanaerobacter tengcongensis

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