GTP cyclohydrolase I from Tetrahymena pyriformis

Cloning of cDNA and expression

Masahiro Tazawa, Masatsugu Ohtsuki, Chiho Ichinose, Hiroaki Shiraishi, Risa Kuroda, Yasumichi Hagino, Shigeru Nakashima, Yoshinori Nozawa, Hiroshi Ichinose, Toshiharu Nagatsu, Takahide Nomura

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)65-73
Number of pages9
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume127
Issue number1
DOIs
Publication statusPublished - 01-09-2000

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GTP Cyclohydrolase
Tetrahymena pyriformis
Cloning
Organism Cloning
Complementary DNA
Messenger RNA
Cells
Tetrahymena
Amino Acids
Dictyostelium
Molecular mass
Drosophila melanogaster
Gene Library
Cell Division
Yeast
Escherichia coli
Sequence Analysis
Saccharomyces cerevisiae
Rats
Amino Acid Sequence

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology

Cite this

Tazawa, Masahiro ; Ohtsuki, Masatsugu ; Ichinose, Chiho ; Shiraishi, Hiroaki ; Kuroda, Risa ; Hagino, Yasumichi ; Nakashima, Shigeru ; Nozawa, Yoshinori ; Ichinose, Hiroshi ; Nagatsu, Toshiharu ; Nomura, Takahide. / GTP cyclohydrolase I from Tetrahymena pyriformis : Cloning of cDNA and expression. In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 2000 ; Vol. 127, No. 1. pp. 65-73.
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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 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.",
author = "Masahiro Tazawa and Masatsugu Ohtsuki and Chiho Ichinose and Hiroaki Shiraishi and Risa Kuroda and Yasumichi Hagino and Shigeru Nakashima and Yoshinori Nozawa and Hiroshi Ichinose and Toshiharu Nagatsu and Takahide Nomura",
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Tazawa, M, Ohtsuki, M, Ichinose, C, Shiraishi, H, Kuroda, R, Hagino, Y, Nakashima, S, Nozawa, Y, Ichinose, H, Nagatsu, T & Nomura, T 2000, 'GTP cyclohydrolase I from Tetrahymena pyriformis: Cloning of cDNA and expression', Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, vol. 127, no. 1, pp. 65-73. https://doi.org/10.1016/S0305-0491(00)00239-X

GTP cyclohydrolase I from Tetrahymena pyriformis : Cloning of cDNA and expression. / Tazawa, Masahiro; Ohtsuki, Masatsugu; Ichinose, Chiho; Shiraishi, Hiroaki; Kuroda, Risa; Hagino, Yasumichi; Nakashima, Shigeru; Nozawa, Yoshinori; Ichinose, Hiroshi; Nagatsu, Toshiharu; Nomura, Takahide.

In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 127, No. 1, 01.09.2000, p. 65-73.

Research output: Contribution to journalArticle

TY - JOUR

T1 - GTP cyclohydrolase I from Tetrahymena pyriformis

T2 - Cloning of cDNA and expression

AU - Tazawa, Masahiro

AU - Ohtsuki, Masatsugu

AU - Ichinose, Chiho

AU - Shiraishi, Hiroaki

AU - Kuroda, Risa

AU - Hagino, Yasumichi

AU - Nakashima, Shigeru

AU - Nozawa, Yoshinori

AU - Ichinose, Hiroshi

AU - Nagatsu, Toshiharu

AU - Nomura, Takahide

PY - 2000/9/1

Y1 - 2000/9/1

N2 - 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.

AB - 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.

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U2 - 10.1016/S0305-0491(00)00239-X

DO - 10.1016/S0305-0491(00)00239-X

M3 - Article

VL - 127

SP - 65

EP - 73

JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

SN - 1096-4959

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