GTP cyclohydrolase I from Tetrahymena pyriformis: cloning of cDNA and expression
A full-length cDNA clone for GTP cyclohydrolase I (EC 3.5.4.16) was isolated from a Tetrahymena pyriformis cDNA library by plaque hybridization. The nucleotide sequence determination revealed that the length of the cDNA insert was 1516 bp. The coding region encoded a protein of 223 amino acid residu...
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Veröffentlicht in: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2000-09, Vol.127 (1), p.65-73 |
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Sprache: | eng |
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Zusammenfassung: | A full-length cDNA clone for GTP cyclohydrolase I (EC 3.5.4.16) was isolated from a
Tetrahymena pyriformis cDNA library by plaque hybridization. The nucleotide sequence determination revealed that the length of the cDNA insert was 1516 bp. The coding region encoded a protein of 223 amino acid residues with a calculated molecular mass of 25 416 Da. The deduced amino acid sequence of
Tetrahymena GTP cyclohydrolase I showed sequence identity with that of
Escherichia coli (55%). The identity of
T. pyriformis GTP cyclohydrolase I with sequences of
Dictyostelium discoideum,
Saccharomyces cerevisiae,
Drosophila melanogaster, mouse, rat, and human enzymes was less marked and was 30, 30, 25, 28, 28, and 27%, respectively. RNA blot analysis showed a single mRNA species of 2.1 kb in this protozoan. The mRNA level of GTP cyclohydrolase I increased during synchronous cell division induced by intermittent heat treatment. The results suggest that the mRNA expression is associated with the cell cycle of
T. pyriformis. |
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ISSN: | 1096-4959 1879-1107 |
DOI: | 10.1016/S0305-0491(00)00239-X |