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Cloning and sequencing the genomic encoding region of copper–zinc superoxide dismutase enzyme from several marine strains of the genus Debaryomyces (Lodder & Kreger‐van Rij)
Author(s) -
HernándezSaavedra Norma Y.,
RomeroGeraldo Reyna
Publication year - 2001
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.768
Subject(s) - biology , biochemistry , superoxide dismutase , amino acid , peptide sequence , enzyme , nucleic acid sequence , yeast , sod1 , gene
Copper–zinc superoxide dismutase (SODC) is a cytosolic enzyme which catalyses the dismutation of the superoxide radical. Due to its physiological importance, the encoding genes have been cloned from several species of higher eukaryotes. However, genes from moulds and yeast have not been studied extensively. In this paper, the encoding region of this gene ( sod1 ) has been cloned from several strains of marine yeast belonging to the genus Debaryomyces (dvv sod1, dvy sod1 and dh sod1 ‐61) through genomic DNA–PCR amplification. Fragments of 480–486 nucleotides were obtained, which contain information for products of 153–156 amino acids with calculated molecular masses of 15.8–16.6 kDa. The deduced amino acid sequence shows that D. vanrijiae enzymes present three additional amino acids not closely related to the active site conformation. In addition, in D. vanrijiae var. vanrijiae (strain 020), one histidine residue is apparently replaced by a proline; the incidence and function of other aromatic or heterocyclic amino acids is discussed. Homology and phylogenetic trees were constructed from amino‐acid sequence multi‐alignment analyses; the interrelationships among fungi are discussed. The sod‐1 sequences reported in this paper were deposited in the public data library of the NCBI under Accession Nos AF301019, AF327449 and AF327448. Copyright © 2001 John Wiley & Sons, Ltd.

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