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Characterization of Candida albicans orthologue of the Saccharomyces cerevisiae signal‐peptidase‐subunit encoding gene SPC3
Author(s) -
De la Rosa José M.,
González José M.,
Gutiérrez Fernando,
Ruíz Teresa,
Rodríguez Luis
Publication year - 2004
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.1137
Subject(s) - biology , signal peptidase , complementation , saccharomyces cerevisiae , mutant , gene , translocon , candida albicans , genetics , signal peptide , microbiology and biotechnology , peptide sequence , chromosomal translocation
Abstract The Candida albicans orthologue of the SPC3 gene, which encodes one of the subunits essential for the activity of the signal peptidase complex in Saccharomyces cerevisiae , was isolated by complementation of a thermosensitive mutation in the S. cerevisiae SEC61 gene. The cloned gene ( CaSPC3 ) encodes a putative protein of 192 amino acids that contains one potential membrane‐spanning region and shares significant homology with the corresponding products from mammalian (Spc22/23p) and yeast (Spc3p) cells. CaSPC3 is essential for cell viability, since a hemizygous strain containing a single copy of CaSPC3 under control of the methionine‐repressible MET3 promoter did not grow in the presence of methionine and cysteine. The cloned gene could rescue the phenotype associated with a spc3 mutation in S. cerevisiae , indicating that it is the true C. albicans orthologue of SPC3 . However, in contrast with results previously described for its S. cerevisiae orthologue, CaSPC3 was not able to complement the thermosensitive growth associated with a mutation in the SEC11 gene. The heterologous complementation of the sec61 mutant suggests that Spc3p could play a role in the interaction that it is known to occur between the translocon (Sec61 complex) and the signal peptidase complex, at the endoplasmic reticulum membrane. Copyright © 2004 John Wiley & Sons, Ltd.

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