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Telomeres from  Drosophila  appear to be very different from those of other organisms – in size and the mechanism of their maintenance. In the absence of the enzyme telomerase,  Drosophila  telomeres are maintained by retrotransposition of three elements,  HeT-A ,  TART , and  TAHRE , but details of their transposition mechanisms are not known. Here we characterized some biochemical characteristics of the  HeT-A  Gag protein encoded by the  HeT-A  element to understand this mechanism. The  HeT-A  Gag protein when overexpressed in S2 cells was localized to the nucleus but was resistant to high salt, detergents and nuclease extraction treatments. Analysis of the  HeT-A  Gag protein by tandem mass spectrophotometry revealed that serines 216 and 221 are phosphorylated. Substituting these serines with alanine or aspartic acid by site-directed mutagenesis did not result in any changes in  HeT-A  Gag translocation across the nucleus, suggesting that phosphorylation of these sites is not associated with  HeT-A  Gag translocation, but time course experiments showed that these phosphorylation sites are important for Gag-protein stability.

Phosphorylation at Serines 216 and 221 Is Important for Drosophila HeT-A Gag Protein Stability