Masahiro Tazawa, Masatsugu Ohtsuki, Chiho Sumi-Ichinose, Hiroaki Shiraishi, Risa Kuroda, Yasumichi Hagino, Shigeru Nakashima, Yoshinori Nozawa, Yoshinori Nozawa, Hiroshi Ichinose, Toshiharu Nagatsu, Takahide Nomura
Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology 127 65-73
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. (C) 2000 Elsevier Science Inc.