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KTR2 : A new member of the KRE2 mannosyltransferase gene family
Author(s) -
Lussier Marc,
Camirand Anne,
Sdicu AnneMarie,
Bussey Howard
Publication year - 1993
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.320091004
Subject(s) - biology , mannose , mutant , gene , saccharomyces cerevisiae , glycosylation , genetics , microbiology and biotechnology , gene product , gene family , locus (genetics) , biochemistry , gene expression
The KTR2 gene from Saccharomyces cerevisiae was identified by polymerase chain reaction amplification of genomic DNA using primers derived from regions of high homology between the products of three yeast genes, KRE2, YUR1 and KTR1 . The product encoded by the KTR2 gene is a predicted type II membrane protein of 425 amino acid residues with a short cytoplasmic N‐terminus, a membrane‐spanning region and a large lumenal domain containing four potential N‐glycosylation sites. Ktr2p has 58% identity with Yur1p, 39% with Ktr1p and 34% with Kre2p. One member of this gene family, KRE2 (also known as MNT1 ; Häusler and Robbins, 1992), encodes an α‐1,2 mannosyltransferase which adds the third mannose onto O‐linked glycoprotein side‐chains (Häusler et al. , 1992). In contrast to KRE2 null mutants, which produce shortened (two‐mannose) chains, mutants harboring a KTR2 gene disruption synthesize O‐linked chains with the wild‐type patterns of five mannose residues. A null mutation in KTR2 leads to partial resistance to killer toxin and hints that KTR2 , which encodes a putative mannosyltransferase, is involved in extracellular matrix assembly.