| RRC ID |
75043
|
| 著者 |
Ohashi T, Tanaka T, Tanaka N, Takegawa K.
|
| タイトル |
SpMnn9p and SpAnp1p form a protein complex involved in mannan synthesis in the fission yeast Schizosaccharomyces pombe.
|
| ジャーナル |
J Biosci Bioeng
|
| Abstract |
The cell walls of yeast cells possess a large mannan structure mainly comprising of a linear α1,6-linked mannose oligomer on the N-linked glycans. The biosynthesis of the mannan is initiated by ScOch1p α1,6-mannosyltransfease, and elongated by the mannan polymerase complexes M-Pol I and II in the Golgi of Saccharomyces cerevisiae. Here, we functionally characterized SpMnn9 and SpAnp1 proteins in the fission yeast Schizosaccharomyces pombe; these proteins are homologs of S. cerevisiae M-Pol II complex proteins ScMnn9p and ScAnp1p. Cells harboring disruptions in Spmnn9+ and Spanp1+ genes showed slower growth at 37°C and an increased sensitivity to hygromycin B, characteristic of a glycosylation defect. Results obtained from the acid phosphatase assay and high-performance liquid chromatography analysis of N-linked glycans in Spmnn9Δ and Spanp1Δ mutants suggested that the mannan structure in S. pombe is synthesized sequentially by the α-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p. Immunoprecipitation and split YFP analyses demonstrated that SpMnn9p and SpAnp1p form the M-Pol-II like complex. Together, these results provided an improved understanding of the mechanism of mannan synthesis by SpMnn9p and SpAnp1p in S. pombe.
|
| 巻・号 |
130(4)
|
| ページ |
335-340
|
| 公開日 |
2020-10-1
|
| DOI |
10.1016/j.jbiosc.2020.06.003
|
| PII |
S1389-1723(20)30254-1
|
| PMID |
32650974
|
| MeSH |
Cell Wall / metabolism
Glycosylation
Golgi Apparatus / metabolism
Mannans / biosynthesis*
Mannosyltransferases / metabolism
Schizosaccharomyces / cytology
Schizosaccharomyces / metabolism*
Schizosaccharomyces pombe Proteins / genetics
Schizosaccharomyces pombe Proteins / metabolism*
|
| IF |
2.366
|
| リソース情報 |
| 酵母 |
Wild-type S. pombe ARC039 |
