Nucleotide sequence of the phosphoglycerate kinase gene from the extreme thermophile Thermus thermophilus. Comparison of the deduced amino acid sequence with that of the mesophilic yeast phosphoglycerate kinase

Using oligonucleotide probes derived from amino acid sequencing information, the structural gene for phosphoglycerate kinase from the extreme thermophile, Thermus thermophilus, was cloned in Escherichia coli and its complete nucleotide sequence determined. The gene consists of an open reading frame...

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Bibliographic Details
Published in:Biochemical journal 1988-09, Vol.254 (2), p.509-517
Main Authors: Bowen, D, Littlechild, J A, Fothergill, J E, Watson, H C, Hall, L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Electrophoresis, Agar Gel
Molecular Sequence Data
Phosphoglycerate Kinase - genetics
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Thermus - enzymology
Thermus - genetics
Thermus thermophilus
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Summary:Using oligonucleotide probes derived from amino acid sequencing information, the structural gene for phosphoglycerate kinase from the extreme thermophile, Thermus thermophilus, was cloned in Escherichia coli and its complete nucleotide sequence determined. The gene consists of an open reading frame corresponding to a protein of 390 amino acid residues (calculated Mr 41,791) with an extreme bias for G or C (93.1%) in the codon third base position. Comparison of the deduced amino acid sequence with that of the corresponding mesophilic yeast enzyme indicated a number of significant differences. These are discussed in terms of the unusual codon bias and their possible role in enhanced protein thermal stability.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2540509