Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box - PubMed
Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box
M Kiledjian et al. EMBO J. 1992 Jul.
Abstract
Heterogeneous nuclear ribonucleoproteins (hnRNPs) are thought to influence the structure of hnRNA and participate in the processing of hnRNA to mRNA. The hnRNP U protein is an abundant nucleoplasmic phosphoprotein that is the largest of the major hnRNP proteins (120 kDa by SDS-PAGE). HnRNP U binds pre-mRNA in vivo and binds both RNA and ssDNA in vitro. Here we describe the cloning and sequencing of a cDNA encoding the hnRNP U protein, the determination of its amino acid sequence and the delineation of a region in this protein that confers RNA binding. The predicted amino acid sequence of hnRNP U contains 806 amino acids (88,939 Daltons), and shows no extensive homology to any known proteins. The N-terminus is rich in acidic residues and the C-terminus is glycine-rich. In addition, a glutamine-rich stretch, a putative NTP binding site and a putative nuclear localization signal are present. It could not be defined from the sequence what segment of the protein confers its RNA binding activity. We identified an RNA binding activity within the C-terminal glycine-rich 112 amino acids. This region, designated U protein glycine-rich RNA binding region (U-gly), can by itself bind RNA. Furthermore, fusion of U-gly to a heterologous bacterial protein (maltose binding protein) converts this fusion protein into an RNA binding protein. A 26 amino acid peptide within U-gly is necessary for the RNA binding activity of the U protein. Interestingly, this peptide contains a cluster of RGG repeats with characteristic spacing and this motif is found also in several other RNA binding proteins. We have termed this region the RGG box and propose that it is an RNA binding motif and a predictor of RNA binding activity.
Similar articles
-
Ghetti A, Piñol-Roma S, Michael WM, Morandi C, Dreyfuss G. Ghetti A, et al. Nucleic Acids Res. 1992 Jul 25;20(14):3671-8. doi: 10.1093/nar/20.14.3671. Nucleic Acids Res. 1992. PMID: 1641332 Free PMC article.
-
Görlach M, Burd CG, Dreyfuss G. Görlach M, et al. J Biol Chem. 1994 Sep 16;269(37):23074-8. J Biol Chem. 1994. PMID: 8083209
-
Swanson MS, Nakagawa TY, LeVan K, Dreyfuss G. Swanson MS, et al. Mol Cell Biol. 1987 May;7(5):1731-9. doi: 10.1128/mcb.7.5.1731-1739.1987. Mol Cell Biol. 1987. PMID: 3110598 Free PMC article.
-
Chaudhury A, Chander P, Howe PH. Chaudhury A, et al. RNA. 2010 Aug;16(8):1449-62. doi: 10.1261/rna.2254110. Epub 2010 Jun 28. RNA. 2010. PMID: 20584894 Free PMC article. Review.
-
The roles of heterogeneous nuclear ribonucleoproteins (hnRNP) in RNA metabolism.
Weighardt F, Biamonti G, Riva S. Weighardt F, et al. Bioessays. 1996 Sep;18(9):747-56. doi: 10.1002/bies.950180910. Bioessays. 1996. PMID: 8831291 Review.
Cited by
-
The new (dis)order in RNA regulation.
Järvelin AI, Noerenberg M, Davis I, Castello A. Järvelin AI, et al. Cell Commun Signal. 2016 Apr 6;14:9. doi: 10.1186/s12964-016-0132-3. Cell Commun Signal. 2016. PMID: 27048167 Free PMC article. Review.
-
RNA-binding proteins in pluripotency, differentiation, and reprogramming.
Guallar D, Wang J. Guallar D, et al. Front Biol (Beijing). 2014 Oct;9(5):389-409. doi: 10.1007/s11515-014-1326-y. Front Biol (Beijing). 2014. PMID: 25554730 Free PMC article.
-
Protein conformation and biomolecular condensates.
Vazquez DS, Toledo PL, Gianotti AR, Ermácora MR. Vazquez DS, et al. Curr Res Struct Biol. 2022 Sep 14;4:285-307. doi: 10.1016/j.crstbi.2022.09.004. eCollection 2022. Curr Res Struct Biol. 2022. PMID: 36164646 Free PMC article. Review.
-
Multi-disciplinary methods to define RNA-protein interactions and regulatory networks.
Ascano M, Gerstberger S, Tuschl T. Ascano M, et al. Curr Opin Genet Dev. 2013 Feb;23(1):20-8. doi: 10.1016/j.gde.2013.01.003. Epub 2013 Feb 28. Curr Opin Genet Dev. 2013. PMID: 23453689 Free PMC article. Review.
-
Boonanuntanasarn S, Bunlipatanon P, Ichida K, Yoohat K, Mengyu O, Detsathit S, Yazawa R, Yoshizaki G. Boonanuntanasarn S, et al. Fish Physiol Biochem. 2016 Dec;42(6):1621-1636. doi: 10.1007/s10695-016-0245-z. Epub 2016 Jul 12. Fish Physiol Biochem. 2016. PMID: 27406385
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases