Literature DB >> 11126753

GTP cyclohydrolase I from Tetrahymena pyriformis: cloning of cDNA and expression.

M Tazawa1, M Ohtsuki, C Sumi-Ichinose, H Shiraishi, R Kuroda, Y Hagino, S Nakashima, Y Nozawa, H Ichinose, T Nagatsu, T Nomura.   

Abstract

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 Tetrahrymena 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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Year:  2000        PMID: 11126753     DOI: 10.1016/s0305-0491(00)00239-x

Source DB:  PubMed          Journal:  Comp Biochem Physiol B Biochem Mol Biol        ISSN: 1096-4959            Impact factor:   2.231


  1 in total

1.  A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions.

Authors:  Lance Swick; Gregory Kapatos
Journal:  J Neurochem       Date:  2006-06       Impact factor: 5.372

  1 in total

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