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Schizosaccharomyces pombe och1 + encodes α‐1,6‐mannosyltransferase that is involved in outer chain elongation of N ‐linked oligosaccharides
Author(s) -
Yoko-o Takehiko,
Tsukahara Kappei,
Watanabe Tatsuo,
Hata-Sugi Naoko,
Yoshimatsu Kentaro,
Nagasu Takeshi,
Jigami Yoshifumi
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02082-8
Subject(s) - schizosaccharomyces pombe , mannose , biochemistry , saccharomyces cerevisiae , mutant , yeast , schizosaccharomyces , gene product , gene , chemistry , biology , gene expression
The fission yeast Schizosaccharomyces pombe attaches an outer chain containing mannose and galactose to the N ‐linked oligosaccharides on many of its glycoproteins. We identified an S. pombe och1 mutant that did not synthesize the outer chains on acid phosphatase. The S. pombe och1 + gene was a functional homolog of Saccharomyces cerevisiae OCH1 , and its gene product (SpOch1p) incorporated α‐1,6‐linked mannose into pyridylaminated Man 9 GlcNAc 2 , indicating that och1 + encodes an α‐1,6‐mannosyltransferase. Our results indicate that SpOch1p is a key enzyme of outer chain elongation. The substrate specificity of SpOch1p was different from that of S. cerevisiae OCH1 gene product (ScOch1p), suggesting that SpOch1p may have a wider substrate specificity than that of ScOch1p.