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Comparative functional analysis of the OCH1 mannosyltransferase families in Aspergillus fumigatus and Saccharomyces cerevisiae
Author(s) -
Lambou Karine,
Perkhofer Susanne,
Fontaine Thierry,
Latge JeanPaul
Publication year - 2010
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.1798
Subject(s) - aspergillus fumigatus , biology , saccharomyces cerevisiae , mannan , hygromycin b , mutant , glycosylation , gene , phenotype , microbiology and biotechnology , biochemistry , genetics , polysaccharide
α1,6‐linked mannans are an essential component of the Aspergillus fumigatus galactomannan, which is either GPI‐anchored to the plasma membrane or covalently bound to the polysaccharide core of the cell wall. In Saccharomyces cerevisiae , the OCH1 gene encodes an α1,6‐mannosyltransferase that initiates the synthesis of the α1,6 linked‐mannan. In the A. fumigatus genome, four orthologous genes of Saccharomyces cerevisiae ScOCH1 gene were identified. Single deletion and the quadruple deletion mutants ( Afoch1‐4Δ ) were constructed in A. fumigatus . No phenotype different from the wild‐type strain was observed in all single and the quadruple mutants. The corresponding cDNAs of the AfOCH1‐4 A. fumigatus orthologues were expressed in the S. cerevisiae Scoch1Δ mutant. Among the four orthologues, only AfOCH1 complemented the aggregation phenotype, the growth inhibition, the hypersensitivity to hygromycin and the protein glycosylation defects observed in the Scoch1Δ mutant. Copyright © 2010 John Wiley & Sons, Ltd.