Schizosaccharomyces pombe och1+ encodes α‐1,6‐mannosyltransferase that is involved in outer chain elongation of N‐linked oligosaccharides
- 26 January 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 489 (1) , 75-80
- https://doi.org/10.1016/s0014-5793(01)02082-8
Abstract
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 Man9GlcNAc2, 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.Keywords
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