Open AccessSequence of the Saccharomyces cerevisiae CATI gene and amino acid sequence of catalase A derived from it
Author(s) -
CHOEN Gerald,
RAPATZ Winfried,
RUIS Helmut
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb14263.x
Subject(s) - peroxisome , saccharomyces cerevisiae , catalase , candida tropicalis , biochemistry , peptide sequence , amino acid , nucleic acid sequence , biology , open reading frame , peroxisomal targeting signal , enzyme , microbiology and biotechnology , yeast , gene
The nucleotide sequence of a 2785‐base‐pair stretch of DNa containing the Saccharomyces cerevisiae catalase A (CATI) 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 tothe 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 betwen 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.