Sequence of the Saccharomyces cerevisiae CATI gene and amino acid sequence of catalase A derived from it
- 1 September 1988
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 176 (1), 159-163
- https://doi.org/10.1111/j.1432-1033.1988.tb14263.x
Abstract
The nucleotide sequence of a 2785-base-pair stretch of DNA containing the Saccharomyces cerevisiae catalase A(CTA1) gene has been determined. This gene contains an uninterrupted open reading frame encoding a protein of 515 amino acids (relative molecular mass 58490). Catalase A, the peroxisomal catalase of S. cerevisiae was compared to the peroxisomal catalases from bovine liver and from Candida tropicalis and to the non-peroxisomal, presumably cytoplasmic, catalase T of S. cerevisiae. Whereas the peroxisomal catalases are almost colinear, three major insertions have to be introduced in the catalase T sequence to obtain an optimal fit with the other proteins. Catalase A is most closely related to the C. tropicalis enzyme. It is also more similar to the bovine liver catalase than to the second S. cerevisiae catalase. The differences between the two S. cerevisiae enzymes are most striking within four blocks of amino acids consisting of a total of 37 residues with high homology between the three peroxisomal, but low conservation between the S. cerevisiae catalases. The results obtained indicate that the peroxisomal catalases compared have very similar three-dimensional structures and might have similar targetting signals.This publication has 44 references indexed in Scilit:
- Catalase gene of the yeast Candida tropicalisEuropean Journal of Biochemistry, 1987
- Yeast HAP1 activator competes with the factor RC2 for binding to the upstream activation site UAS1 of the CYC1 geneCell, 1987
- Yeast HAP1 activator binds to two upstream activation sites of different sequenceCell, 1987
- A C-terminal signal prevents secretion of luminal ER proteinsCell, 1987
- Nucleotide sequence of the Saccharomyces cerevisiae CTT1 gene and deduced amino‐acid sequence of yeast catalase TEuropean Journal of Biochemistry, 1986
- The refined structure of beef liver catalase at 2·5 Å resolutionActa crystallographica Section B, Structural science, crystal engineering and materials, 1986
- The active center of catalaseJournal of Molecular Biology, 1985
- Structure of beef liver catalaseJournal of Molecular Biology, 1981
- Synthesis of Saccharomyces cerevisiae Catalase A in vitroEuropean Journal of Biochemistry, 1981
- Localization of Catalase A in Vacuoles ofSaccharomyces cerevisiae:Evidence for the Vacuolar Nature of Isolated "Yeast Peroxisomes"Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976