Separable Roles in Vivo for the Two RNA Binding Domains of Drosophila A1-hnRNP Homolog
Overview
Affiliations
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.
The hnRNP A1 homolog Hrb87F/Hrp36 is important for telomere maintenance in Drosophila melanogaster.
Singh A, Lakhotia S Chromosoma. 2015; 125(3):373-88.
PMID: 26373285 DOI: 10.1007/s00412-015-0540-y.
Specification of the somatic musculature in Drosophila.
Dobi K, Schulman V, Baylies M Wiley Interdiscip Rev Dev Biol. 2015; 4(4):357-75.
PMID: 25728002 PMC: 4456285. DOI: 10.1002/wdev.182.
Khan F, Daniels M, Folkers G, Boelens R, Naqvi S, Ingen H Nucleic Acids Res. 2014; 42(13):8705-18.
PMID: 24957607 PMC: 4117745. DOI: 10.1093/nar/gku468.
HnRNP A1 controls a splicing regulatory circuit promoting mesenchymal-to-epithelial transition.
Bonomi S, Di Matteo A, Buratti E, Cabianca D, Baralle F, Ghigna C Nucleic Acids Res. 2013; 41(18):8665-79.
PMID: 23863836 PMC: 3794575. DOI: 10.1093/nar/gkt579.
Singh A, Lakhotia S J Biosci. 2012; 37(4):659-78.
PMID: 22922191 DOI: 10.1007/s12038-012-9239-x.