In mice, megl is a meiosis expressed gene in both males and females. In the teslis. its protein product, Megl. is very abundant and consists of about 40-50 percent of all coomassie blue stained proteins in a gol of testicuhir cell lysale. This protein appears in multiple phosphorylated forms, including two dimeric forms of 31 arid 32 kDa. Immunoprecipitation and iinmunoblotting experiments, using specific antiphosphoamino acid antibodies, revealed that the 31 kDa form is tyrosine but not serine and threonine phosphorylated whereas the 32 kDa form is serine and threonine but not tyrosine phosphorylated. These two forms show a developmentally regulated switch that correlates with entry into nieiotic differentiation. Immunoblotting as well as immunohisiochernical analysis revealed that Megl is a nuclear protein that shows DNA binding properties. Megl seems to bind UNA in a non sequence specific manner or alternatively, it binds to highly redundant sequences. Based on Megl's abundancy. the meiotic specificity and the non sequence specific DNA binding properties, a tempting reasonable speculation would be that Megl plays a role in organizing meiotic chromatin and that dimerization and phosphorvlation / dephosphorylation reactions are important to its function.
|State||Published - 1997|