Mpg2 interacts and cooperates with Mpg1 to maintain yeast glycosylation

作者：Cruz Munoz Centeno M; Martin Guevara Carlos; Flores Amando; Perez Pulido Antonio J; Antunez Rodriguez Cristina; Castillo Araceli G; Sanchez Duran Miguel; Mier Pablo; Bejarano Eduardo R

来源：FEMS Yeast Research, 2012, 12(5): 511-520.

DOI：10.1111/j.1567-1364.2012.00801.x

• glycosylation
• GDP-mannose-1-phosphate guanylyltransferases
• genetic interactions
• yeast cell cycle progression

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 ?mpg2 mutant phenotypes. Taken together, these results indicate that mpg1 and mpg2 function together in glycosylation and septum formation.

• 出版日期2012-8