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Mpg2 interacts and cooperates with Mpg1 to maintain yeast glycosylation.

FEMS yeast research (2012-03-16)
M Cruz Muñoz-Centeno, Carlos Martín-Guevara, Amando Flores, Antonio J Pérez-Pulido, Cristina Antúnez-Rodríguez, Araceli G Castillo, Miguel Sanchez-Durán, Pablo Mier, Eduardo R Bejarano
ABSTRACT

Using a yeast two-hybrid screen, we isolated a gene from Schizosaccharomyces pombe, whose product interacts with Mpg1, a GDP-mannose-1-phosphate guanylyltransferase involved in the maintenance of cell wall integrity and glycosylation. We have designated this gene mpg2 based on its similarity to Mpg1. Mpg2 is evolutionarily conserved in higher eukaryotes. In the absence of Mpg2, defects in cell growth and sensitivity to hygromycin B are observed. When mpg1 is depleted, the lack of mpg2 causes a synthetic enhancement of the growth defect, the sensitivity to hygromycin B and the cell cycle phenotype previously reported for mpg1 mutant. Finally, Mpg1 overexpression complements the Δmpg2 mutant phenotypes. Taken together, these results indicate that mpg1 and mpg2 function together in glycosylation and septum formation.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Hygromycin B from Streptomyces hygroscopicus, lyophilized powder
Sigma-Aldrich
Hygromycin B from Streptomyces hygroscopicus, suitable for plant cell culture, BioReagent, ≥60% (HPLC), lyophilized powder
Sigma-Aldrich
Hygromycin B from Streptomyces hygroscopicus, powder, BioReagent, suitable for cell culture, suitable for insect cell culture
Sigma-Aldrich
Hygromycin B solution from Streptomyces hygroscopicus, ≥60% (HPLC), 45-60 mg/mL in H2O
Sigma-Aldrich
Hygromycin B solution from Streptomyces hygroscopicus, ≥60% (HPLC), 45-60 mg/mL in H2O, γ-irradiated