TY - JOUR
T1 - Characterization of O-mannosyltransferase family in Schizosaccharomyces pombe
AU - Tanaka, Naotaka
AU - Fujita, Yasuko
AU - Suzuki, Shotaro
AU - Morishita, Masayo
AU - Giga-Hama, Yuko
AU - Shimoda, Chikashi
AU - Takegawa, Kaoru
N1 - Funding Information:
We thank Taro Nakamura for providing S. pombe strains and plasmids. We thank Dr. M Tabuchi (University of California, San Diego) for plasmid pFML1. This work was partly supported by a Grant-in-Aid for Scientific Research from the Japanese Ministry of Education, Science and Culture (to N.T. and K.T.), and by the New Energy and Industrial Technology Development Organization (to K.T.).
PY - 2005/5/13
Y1 - 2005/5/13
N2 - Protein O-glycosylation is an essential protein modification in eukaryotic cells. In Saccharomyces cerevisiae, O-mannosylation is initiated in the lumen of the endoplasmic reticulum by O-mannosyltransferase gene products (Pmt1p-7p). A search of the Schizosaccharomyces pombe genome database revealed a total of three O-glycoside mannosyltransferase homologs (ogm1+, ogm2 +, and ogm4+), closely related to Saccharomyces cerevisiae PMT1, PMT2, and PMT4. Although individual ogm genes were not found to be essential, ogm1Δ and ogm4Δ mutants exhibited aberrant morphology and failed to agglutinate during mating. The phenotypes of the ogm4Δ mutant were not complemented by overexpression of ogm1+ or ogm2+, suggesting that each of the Ogm proteins does not have overlapping functions. Heterologous expression of a chitinase from S. cerevisiae in the ogm mutants revealed that O-glycosylation of chitinase had decreased in ogm1Δ cells. A GFP-tagged Fus1p from S. cerevisiae was specifically not glycosylated and accumulated in the Golgi in ogm4Δ cells. These results indicate that O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins in S. pombe.
AB - Protein O-glycosylation is an essential protein modification in eukaryotic cells. In Saccharomyces cerevisiae, O-mannosylation is initiated in the lumen of the endoplasmic reticulum by O-mannosyltransferase gene products (Pmt1p-7p). A search of the Schizosaccharomyces pombe genome database revealed a total of three O-glycoside mannosyltransferase homologs (ogm1+, ogm2 +, and ogm4+), closely related to Saccharomyces cerevisiae PMT1, PMT2, and PMT4. Although individual ogm genes were not found to be essential, ogm1Δ and ogm4Δ mutants exhibited aberrant morphology and failed to agglutinate during mating. The phenotypes of the ogm4Δ mutant were not complemented by overexpression of ogm1+ or ogm2+, suggesting that each of the Ogm proteins does not have overlapping functions. Heterologous expression of a chitinase from S. cerevisiae in the ogm mutants revealed that O-glycosylation of chitinase had decreased in ogm1Δ cells. A GFP-tagged Fus1p from S. cerevisiae was specifically not glycosylated and accumulated in the Golgi in ogm4Δ cells. These results indicate that O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins in S. pombe.
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U2 - 10.1016/j.bbrc.2005.03.033
DO - 10.1016/j.bbrc.2005.03.033
M3 - Article
C2 - 15809069
AN - SCOPUS:16244386537
SN - 0006-291X
VL - 330
SP - 813
EP - 820
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -