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Separable Roles in Vivo for the Two RNA Binding Domains of Drosophila A1-hnRNP Homolog

Overview
Journal RNA
Specialty Molecular Biology
Date 1998 Dec 16
PMID 9848655
Citations 12
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Abstract

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 GRD were largely responsible for both the cellular location of the protein and for the typical chromosomal distribution pattern of the protein at sites of PolII transcription. RBD-1 also provided a role in the exon-skipping activity of the protein that was not provided by RBD-2. On the other hand, RBD-2 and the GRD were responsible for the very limited chromosomal distribution pattern seen upon heat shock, when HRB87F/hrp36 is sequestered at heat-shock puff 93D, which encodes a long nucleus-restricted RNA. Thus, these studies indicate that the two RBDs function independently of each other but in concert with the GRD. In addition, the self-association property of the GRD was strikingly evident in these overexpressed proteins.

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References
1.
Buvoli M, Cobianchi F, Bestagno M, Mangiarotti A, Bassi M, Biamonti G . Alternative splicing in the human gene for the core protein A1 generates another hnRNP protein. EMBO J. 1990; 9(4):1229-35. PMC: 551799. DOI: 10.1002/j.1460-2075.1990.tb08230.x. View

2.
Sarkar G, Sommer S . The "megaprimer" method of site-directed mutagenesis. Biotechniques. 1990; 8(4):404-7. View

3.
Scherly D, Boelens W, Dathan N, van Venrooij W, Mattaj I . Major determinants of the specificity of interaction between small nuclear ribonucleoproteins U1A and U2B'' and their cognate RNAs. Nature. 1990; 345(6275):502-6. DOI: 10.1038/345502a0. View

4.
Query C, Keene J . Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA. Proc Natl Acad Sci U S A. 1990; 87(16):6393-7. PMC: 54540. DOI: 10.1073/pnas.87.16.6393. View

5.
Flickinger T, Salz H . The Drosophila sex determination gene snf encodes a nuclear protein with sequence and functional similarity to the mammalian U1A snRNP protein. Genes Dev. 1994; 8(8):914-25. DOI: 10.1101/gad.8.8.914. View