| Structural highlights
Function
PRP19_HUMAN Plays a role in DNA double-strand break (DSB) repair. Binds double-stranded DNA in a sequence-nonspecific manner. Acts as a structural component of the nuclear framework. May also serve as a support for spliceosome binding and activity. Essential for spliceosome assembly in a oligomerization-dependent manner and might also be important for spliceosome stability. May have E3 ubiquitin ligase activity. The PSO4 complex is required in the DNA interstrand cross-links (ICLs) repair process. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
Human Pre-mRNA Processing factor 19 (hPRPF19) is an important component in human spliceosome machinery. hPRPF19 contains a WD40 repeats domain at its C-terminus, which is also conserved in yeast. Here we determined the crystal structure of the C-terminal WD40 repeat domain of hPRPF19 by X-ray crystallography. Our structural analysis revealed some significantly different structure features between the human and yeast Prp19 WD40 repeat domain. However, there are also conserved clusters of residues at the bottom surface of the fourth and the fifth WD40 repeats, which provides the important implication for the conserved Prp19 proteins in both human and yeast.
Crystal structure of the WD40 domain of human PRPF19.,Zhang Y, Li Y, Liang X, Zhu Z, Sun H, He H, Min J, Liao S, Liu Y Biochem Biophys Res Commun. 2017 Nov 25;493(3):1250-1253. doi:, 10.1016/j.bbrc.2017.09.145. Epub 2017 Sep 28. PMID:28962858[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gotzmann J, Gerner C, Meissner M, Holzmann K, Grimm R, Mikulits W, Sauermann G. hNMP 200: a novel human common nuclear matrix protein combining structural and regulatory functions. Exp Cell Res. 2000 Nov 25;261(1):166-79. PMID:11082287 doi:10.1006/excr.2000.5025
- ↑ Mahajan KN, Mitchell BS. Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase. Proc Natl Acad Sci U S A. 2003 Sep 16;100(19):10746-51. Epub 2003 Sep 5. PMID:12960389 doi:https://dx.doi.org/10.1073/pnas.1631060100
- ↑ Grillari J, Ajuh P, Stadler G, Loscher M, Voglauer R, Ernst W, Chusainow J, Eisenhaber F, Pokar M, Fortschegger K, Grey M, Lamond AI, Katinger H. SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly. Nucleic Acids Res. 2005 Dec 6;33(21):6868-83. Print 2005. PMID:16332694 doi:33/21/6868
- ↑ Loscher M, Fortschegger K, Ritter G, Wostry M, Voglauer R, Schmid JA, Watters S, Rivett AJ, Ajuh P, Lamond AI, Katinger H, Grillari J. Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome. Biochem J. 2005 Jun 1;388(Pt 2):593-603. PMID:15660529 doi:10.1042/BJ20041517
- ↑ Zhang N, Kaur R, Lu X, Shen X, Li L, Legerski RJ. The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links. J Biol Chem. 2005 Dec 9;280(49):40559-67. Epub 2005 Oct 12. PMID:16223718 doi:M508453200
- ↑ Voglauer R, Chang MW, Dampier B, Wieser M, Baumann K, Sterovsky T, Schreiber M, Katinger H, Grillari J. SNEV overexpression extends the life span of human endothelial cells. Exp Cell Res. 2006 Apr 1;312(6):746-59. Epub 2006 Jan 4. PMID:16388800 doi:S0014-4827(05)00560-4
- ↑ Zhang Y, Li Y, Liang X, Zhu Z, Sun H, He H, Min J, Liao S, Liu Y. Crystal structure of the WD40 domain of human PRPF19. Biochem Biophys Res Commun. 2017 Nov 25;493(3):1250-1253. doi:, 10.1016/j.bbrc.2017.09.145. Epub 2017 Sep 28. PMID:28962858 doi:https://dx.doi.org/10.1016/j.bbrc.2017.09.145
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