Open AccessCharacterization of gdp1 + as encoding a GDPase in the fission yeast Schizosaccharomyces pombe
Author(s) -
Sánchez Raquel,
Franco Alejandro,
Gacto Mariano,
Notario Vicente,
Cansado José
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00698-0
Subject(s) - schizosaccharomyces pombe , fission , schizosaccharomyces , yeast , characterization (materials science) , chemistry , radiochemistry , biology , physics , genetics , nuclear physics , saccharomyces cerevisiae , neutron , optics
We have isolated the gdp1 + gene from Schizosaccharomyces pombe coding for a membrane protein with guanosine diphosphatase (GDPase) activity, which is highly homologous to Golgi GDPases isolated from other yeast species. The gdp1 + product, Gdp1p, displays both GDPase and uridine diphosphatase (UDPase) activities in vitro, with a strong dependence for calcium and manganese cations. The observation of a defect in N ‐glycosylation of invertase in S. pombe Δgdp1 cells together with the ability of gdp1 + to functionally complement the defective O ‐mannosylation of chitinase in Saccharomyces cerevisiae cells disrupted in the GDA1 gene ( gdp1 + homolog), suggests a main role for Gdp1p in protein glycosylation in fission yeast.