| Non-Scientific Abstract Retroviruses infect humans and other organisms
causing various diseases.Among these viruses is the HIV retrovirus which ultimately causes AIDS.
Retroviruses insert their genetic information into the chromosomes of host cells. These viruses can
then use the host cellsą replication machinery to replicate themselves. In order to insert their
genetic information into the host chromosomes, retroviruses must first move into the nucleus. In this
paper, the nuclear localization of HeT-A, a retrotransposable element similar to retroviruses, was
studied.Another protein CG8526 was identified as having possible interactions with the HeT-A protein.
Specifically, this paper addresses the role of CG8526 in the nuclear localization of HeT-A.By better
understanding the mechanisms involved in the nuclear localization of retrotransposable elements such
as HeT-A, breakthroughs in retroviral treatments may be found.
HeT-A, a Drosophila non-long terminal repeat (non-LTR) retrotransposon, is unique because it
retrotransposes itself into heterochromatin regions in chromosomes, thereby extending telomeres. The
localization of CG8526, a Drosophila protein that interacted with HeT-A in a yeast two-hybrid screen,
was characterized in Schneider 2 cells. CG8526 encodes a large-form lysophospholipase that possesses
additional function as an asparaginase. Localization of a CG8526-GFP fusion indicates that CG8526
localizes to discrete conglomerates in the cytoplasm. Staining with organelle markers indicated that
these aggregates are not in lysosomal, ER, or Golgi vesicles. Furthermore, immunofluorescent labeling
of Hsp70 and ubiquitin did not show increased levels in the aggregates.An RNAi knockdown of CG8526 was
performed and resulted in a knockout of a HeT-A-GFP fusion. These results indicate that CG8526 may be
important for HeT-A translation or folding. |
