Separable roles in vivo for the two RNA binding domains of Drosophila A1-hnRNP homolog.

@article{Zu1998SeparableRI,
  title={Separable roles in vivo for the two RNA binding domains of Drosophila A1-hnRNP homolog.},
  author={Kai Zu and Martha L. Sikes and A. L. Beyer},
  journal={RNA},
  year={1998},
  volume={4 12},
  pages={1585-98}
}
We analyzed the roles of the three domains of a Drosophila hnRNP A1 homolog by expression of wild-type and mutant versions of HRB87F/hrp36 in Drosophila melanogaster. HRB87F/hrp36 is one of two Drosophila proteins that is most similar to mammalian A1 hnRNP, and like A1, consists of two copies of the RNA-binding domain (RBD) motif followed by a glycine-rich domain (GRD). The role of the domains in nuclear localization and RNA binding to polytene chromosomal sites was determined. RBD-1 and the… CONTINUE READING