Rendiconti Lincei

, Volume 7, Issue 4, pp 315–322 | Cite as

Cloning and characterization of a cDNA encoding glyceral-dehyde-3-phosphate dehydrogenase from the fission yeast Schizosaccharomyces pombe

  • Ivan Orlandi
  • Laura Popolo
  • Paola Cavadini
  • Marina Vai
  • E. Marrè
Biologia molecolare

Abstract

A cDNA encoding glyceraldehyde-3-phosphate dehydrogenase (GPD) was isolated from the fission yeastSchizosaccharomyces pombe. The nucleotide and the predicted amino acid sequences were determined. A very high degree of homology with different GPD sequences present in the SWISS-PROT data bank was observed in accordance with the evolutionary conservation of this enzyme. Northern analysis and the comparison with other fungal GPD sequences suggest that the cDNA corresponds to an activek expressed gene encoding a functional GPD protein. Finally, codon usage analysis revealed the same codor bias observed tor three highly expressed genes inS. pombe.

Key words

Glyceraldheyde-3-phosphate dehydrogenase Ascomycete Basidiomycete 

Clonuggio e carattenzzazione di un cDNA che codifica per 1a gliceraldeide-3-fosfato deidrogenasi del lievito a fissioneSchizosaccharomyces pombe

Riassunto

Un cDNA che codifica per 1a gliceraldeide-3-rostato deidrogenasi (GPD) è stato isolato dal lievito a tissioneSchizosaccharomyces pombe. Sono state determinate sia 1a sequenza nucleotidica che quella amminoacidica predetta. Un alto grado di omologia è stato riscon-trato con diverse sequenze di GPD presenti nella banca dati SWISS-PROT in accordo con 1a conservativita evolutiva di questo enzima. L’analisi di Northern ed il confronto con altre sequenze di GPD fungine sugge-riscono che il cDNA corrisponde ad un gene espresso attivamente codificante per una GPD funzidnale. In fine, l’analisi dell’uso dei codoni rivela 1a stessa scelta preterenziale osserrata per tre geni altamente espressi inS. pombe.

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Copyright information

© Accademia nazionale dei Lincei 1996

Authors and Affiliations

  • Ivan Orlandi
    • 1
  • Laura Popolo
    • 1
  • Paola Cavadini
    • 1
  • Marina Vai
    • 1
  • E. Marrè
    • 1
  1. 1.Dipartimento di Fisiologia e Biochimica Generali Sezione di Biochimica ComparataUniversità degli Studi di MilanoMilano

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