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PRPF19  -  pre-mRNA processing factor 19

Homo sapiens

Synonyms: NMP200, Nuclear matrix protein 200, PRP19, PRP19/PSO4 homolog, PSO4, ...
 
 
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High impact information on PRPF19

  • During catalytic activation of the spliceosome, snRNP remodeling events occur, leading to the formation of a 35S U5 snRNP that contains a large group of proteins, including Prp19 and CDC5, not found in 20S U5 snRNPs [1].
  • Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase [2].
  • Loss of hPso4 expression induced by siRNA results in accumulation of DSBs, apoptosis, and decreased cell survival after DNA damage [2].
  • A conservative Val-->Ile point mutation in the Prp19p U-box domain leads to pre-mRNA splicing defects in vivo [3].
  • Mutagenesis of residues at this interface, while not perturbing the structure of the U-box, abrogates Prp19p function in vivo [4].
  • Knock-out mice deficient in SNEV (hPRP19/hPSO4) are early embryonic lethal [5]
  • SNEV (hPRP19/hPSO4) prolongs the replicative life span of endothelial cells upon overexpression [6].
 

Biological context of PRPF19

  • The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links [7].
  • In interphase cells, green fluorescent protein-tagged hNMP 200 was predominantly nucleoplasmic [8].
  • During cell division hNMP 200 became irregularly distributed in prophase, sparing regions of condensing chromatin [8].
  • SNEV (hPRP19/hPSO4) is the orthologue of the yeast splicing factor Prp19 [9]. Interfering with self assembly of SNEV (hPRP19/hPSO4) inhibits in vitro splicing as well as spliceosome assembly [4].
  • Importantly, a consistent set of abundant NM proteins, some (e.g. hNMP 200) of which displaying structural features, remained unaffected during apoptosis and might therefore represent constituents of an elementary scaffold [10].
  • SNEV (hPRP19/hPSO4) is a ubiquitin E3 ligase and [11] interacts directly with the proteasome [12].
  • SNEV (hPRP19/hPSO4) heterozygous deletion impairs hematopoietic progenitor cell function [13]
 

Anatomical context of PRPF19

 

Other interactions of PRPF19

  • However, the hNMP 200 primary sequence contained five consensus WD-repeat sequences, indicative of participation and regulatory function in larger protein assemblies [8].
  • In situ hybridizations reveal that centrin, cyclin B, and beta-tubulin mRNAs are present in both sterile and spermatogenous cells, but that transcripts encoding RNA helicase and PRP-19 (a spliceosome component) become localized in spermatogenous cells [14].
  • SNEV (hPRP19/hPSO4) interacts with the novel pre-mRNA splicing factor Blom7 [15]
 

Analytical, diagnostic and therapeutic context of PRPF19

References

  1. A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing. Makarova, O.V., Makarov, E.M., Urlaub, H., Will, C.L., Gentzel, M., Wilm, M., Lührmann, R. EMBO J. (2004) [Pubmed]
  2. Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase. Mahajan, K.N., Mitchell, B.S. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  3. Structural insights into the U-box, a domain associated with multi-ubiquitination. Ohi, M.D., Vander Kooi, C.W., Rosenberg, J.A., Chazin, W.J., Gould, K.L. Nat. Struct. Biol. (2003) [Pubmed]
  4. Structural insights into the U-box, a domain associated with multi-ubiquitination. Ohi, M.D., Vander Kooi, C.W., Rosenberg, J.A., Chazin, W.J., Gould, K.L. Nat. Struct. Biol. (2003) [Pubmed]
  5. Early embryonic lethality of mice lacking the essential protein SNEV. Fortschegger, K., Wagner, B., Voglauer, R., Katinger, H., Sibilia, M., Grillari, J. Mol. Cell. Biol. (2007) [Pubmed]
  6. SNEV overexpression extends the life span of human endothelial cells. Voglauer, R., Chang, M.W., Dampier, B., Wieser, M., Baumann, K., Sterovsky, T., Schreiber, M., Katinger, H., Grillari, J. Exp. Cell. Res. (2006) [Pubmed]
  7. The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links. Zhang, N., Kaur, R., Lu, X., Shen, X., Li, L., Legerski, R.J. J. Biol. Chem. (2005) [Pubmed]
  8. hNMP 200: a novel human common nuclear matrix protein combining structural and regulatory functions. Gotzmann, J., Gerner, C., Meissner, M., Holzmann, K., Grimm, R., Mikulits, W., Sauermann, G. Exp. Cell Res. (2000) [Pubmed]
  9. SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly. Grillari, J., Ajuh, P., Stadler, G., Löscher, M., Voglauer, R., Ernst, W., Chusainow, J., Eisenhaber, F., Pokar, M., Fortschegger, K., Grey, M., Lamond, A.I., Katinger, H. Nucleic Acids Res. (2005) [Pubmed]
  10. Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation. Gerner, C., Gotzmann, J., Fröhwein, U., Schamberger, C., Ellinger, A., Sauermann, G. Cell Death Differ. (2002) [Pubmed]
  11. U box proteins as a new family of ubiquitin-protein ligases. Hatakeyama, S., Yada, M., Matsumoto, M., Ishida, N., Nakayama, K.I. J. Biol. Chem. (2001) [Pubmed]
  12. Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome. Löscher, M., Fortschegger, K., Ritter, G., Wostry, M., Voglauer, R., Schmid, J.A., Watters, S., Rivett, A.J., Ajuh, P., Lamond, A.I., Katinger, H., Grillari, J. Biochem. J. (2005) [Pubmed]
  13. Haploinsufficiency of senescence evasion factor causes defects of hematopoietic stem cells functions. Schraml, E., Voglauer, R., Fortschegger, K., Sibilia, M., Stelzer, I., Grillari, J., Schauenstein, K. Stem. Cells. Dev. (2008) [Pubmed]
  14. Differential segregation and modification of mRNA during spermiogenesis in Marsilea vestita. Tsai, C.W., Van Der Weele, C.M., Wolniak, S.M. Dev. Biol. (2004) [Pubmed]
  15. Blom7alpha is a novel heterogeneous nuclear ribonucleoprotein K homology domain protein involved in pre-mRNA splicing that interacts with SNEVPrp19-Pso4. Grillari, J., Löscher, M., Denegri, M., Lee, K., Fortschegger, K., Eisenhaber, F., Ajuh, P., Lamond, A.I., Katinger, H., Grillari-Voglauer, R. J. Biol. Chem. (2009) [Pubmed]
  16. The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases. Vander Kooi, C.W., Ohi, M.D., Rosenberg, J.A., Oldham, M.L., Newcomer, M.E., Gould, K.L., Chazin, W.J. Biochemistry (2006) [Pubmed]
 
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