Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction - PubMed (original) (raw)
. 1996 Feb 16;256(1):20-30.
doi: 10.1006/jmbi.1996.0065.
Affiliations
- PMID: 8609610
- DOI: 10.1006/jmbi.1996.0065
Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction
U Kühn et al. J Mol Biol. 1996.
Abstract
Subsets of the four RNA binding domains (RBD 1 to 4) in the Xenopus poly-adenylate binding protein (PABP) have distinct affinities and specificities for RNA. RBDs 1 plus 2 exhibit RNA affinity and selectivity equal to the wild-type (WT) protein. RBDs 3 plus 4 have distinct selectivity and about ten-fold reduced affinity for A23, and the isolated RBDs 2 or 3 or 4 exhibit about 100-fold reduced affinity for A23 in comparison to WT. For the full-length protein, independent RNA contacts have been mapped by UV crosslinking with RBDs 1/2 and RBDs 3/4. The carboxy-terminal, non-RBD portion of the protein does not contribute to RNA affinity or selectivity, but confers homodimerization activity on PABP. RBDs 3 and 4 cooperate with the C terminus to gain poly(A) organizing activity, i.e. the ability to form an RNP with multiple, regularly spaced copies of PABP on a poly(A) substrate.
Similar articles
- Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target.
Allain FH, Gilbert DE, Bouvet P, Feigon J. Allain FH, et al. J Mol Biol. 2000 Oct 20;303(2):227-41. doi: 10.1006/jmbi.2000.4118. J Mol Biol. 2000. PMID: 11023788 - Chemical shift mapping of the RNA-binding interface of the multiple-RBD protein sex-lethal.
Lee AL, Volkman BF, Robertson SA, Rudner DZ, Barbash DA, Cline TW, Kanaar R, Rio DC, Wemmer DE. Lee AL, et al. Biochemistry. 1997 Nov 25;36(47):14306-17. doi: 10.1021/bi970830y. Biochemistry. 1997. PMID: 9398148 - Contributions of the RNA-binding and linker domains and RNA structure to the specificity and affinity of the nucleolin RBD12/NRE interaction.
Finger LD, Johansson C, Rinaldi B, Bouvet P, Feigon J. Finger LD, et al. Biochemistry. 2004 Jun 8;43(22):6937-47. doi: 10.1021/bi049904d. Biochemistry. 2004. PMID: 15170331 - Multiple RNA binding domains (RBDs) just don't add up.
Shamoo Y, Abdul-Manan N, Williams KR. Shamoo Y, et al. Nucleic Acids Res. 1995 Mar 11;23(5):725-8. doi: 10.1093/nar/23.5.725. Nucleic Acids Res. 1995. PMID: 7535921 Free PMC article. Review. - New insights into the auxiliary domains of eukaryotic RNA binding proteins.
Biamonti G, Riva S. Biamonti G, et al. FEBS Lett. 1994 Feb 28;340(1-2):1-8. doi: 10.1016/0014-5793(94)80162-2. FEBS Lett. 1994. PMID: 7509757 Review.
Cited by
- Characterization of the Role of Hexamer AGUAAA and Poly(A) Tail in Coronavirus Polyadenylation.
Peng YH, Lin CH, Lin CN, Lo CY, Tsai TL, Wu HY. Peng YH, et al. PLoS One. 2016 Oct 19;11(10):e0165077. doi: 10.1371/journal.pone.0165077. eCollection 2016. PLoS One. 2016. PMID: 27760233 Free PMC article. - The Drosophila poly(A) binding protein-interacting protein, dPaip2, is a novel effector of cell growth.
Roy G, Miron M, Khaleghpour K, Lasko P, Sonenberg N. Roy G, et al. Mol Cell Biol. 2004 Feb;24(3):1143-54. doi: 10.1128/MCB.24.3.1143-1154.2004. Mol Cell Biol. 2004. PMID: 14729960 Free PMC article. - A specific role for the C-terminal region of the Poly(A)-binding protein in mRNA decay.
Simón E, Séraphin B. Simón E, et al. Nucleic Acids Res. 2007;35(18):6017-28. doi: 10.1093/nar/gkm452. Epub 2007 Aug 30. Nucleic Acids Res. 2007. PMID: 17766253 Free PMC article. - Nuclear import of cytoplasmic poly(A) binding protein restricts gene expression via hyperadenylation and nuclear retention of mRNA.
Kumar GR, Glaunsinger BA. Kumar GR, et al. Mol Cell Biol. 2010 Nov;30(21):4996-5008. doi: 10.1128/MCB.00600-10. Epub 2010 Sep 7. Mol Cell Biol. 2010. PMID: 20823266 Free PMC article.