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Article: Identification and characterization of human genes encoding Hprp3p and Hprp4p, interacting components of the spliceosome

TitleIdentification and characterization of human genes encoding Hprp3p and Hprp4p, interacting components of the spliceosome
Authors
Issue Date1997
PublisherOxford University Press. The Journal's web site is located at http://hmg.oxfordjournals.org/
Citation
Human Molecular Genetics, 1997, v. 6 n. 12, p. 2117-2126 How to Cite?
AbstractNuclear RNA splicing occurs in an RNA-protein complex, termed the spliceosome. U4/U6 snRNP is one of four essential small nuclear ribonucleoprotein (snRNP) particles (U1, U2, U5 and U4/U6) present in the spliceosome. U4/U6 snRNP contains two snRNAs (U4 and U6) and a number of proteins. We report here the identification and characterization of two human genes encoding U4/U6-associated splicing factors, Hprp3p and Hprp4p, respectively. Hprp3p is a 77 kDa protein, which is homologous to the Saccharomyces cerevisiae splicing factor Prp3p. Amino acid sequence analysis revealed two putative homologues in Caenorhabditis elegans and Schizosaccharomyces pombe. Polyclonal antibodies against Hprp3p were generated with His-tagged Hprp3p over-produced in Escherichia coli. This splicing factor can co-immunoprecipitate with U4, U6 and U5 snRNAs, suggesting that it is present in the U4/U6 U5 tri-snRNP. Hprp4p is a 58 kDa protein homologous to yeast splicing factor Prp4p. Like yeast Prp4p, the human homologue contains repeats homologous to the β-subunit of G-proteins. These repeats are called WD repeats because there is a highly conserved dipeptide of tryptophan and aspartic acid present at the end of each repeat. The primary amino acid sequence homology between human Hprp4p and yeast Prp4p led to the discovery of two additional WD repeats in yeast Prp4p. Structural homology between these human and yeast splicing factors and the β-subunit of G-proteins has been identified by sequence-similarity comparison and analysis of the protein folding by threading. Structural models of Hprp4p and Prp4p with a seven-blade β-propeller topology have been generated based on the structure of β-transducin. Hprp3p and Hprp4p have been shown to interact with each other and the first 100 amino acids of Hprp3p are not essential for this interaction. These experiments suggest that both Hprp3p and Hprp4p are components of human spliceosomes.
Persistent Identifierhttp://hdl.handle.net/10722/44327
ISSN
2015 Impact Factor: 5.985
2015 SCImago Journal Rankings: 4.288
Other Identifiers
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Aen_HK
dc.contributor.authorFormanKay, Jen_HK
dc.contributor.authorLuo, Yen_HK
dc.contributor.authorLuo, Men_HK
dc.contributor.authorChow, YHen_HK
dc.contributor.authorPlumb, Jen_HK
dc.contributor.authorFriesen, JDen_HK
dc.contributor.authorTsui, LCen_HK
dc.contributor.authorHeng, HHQen_HK
dc.contributor.authorWoolford Jr, JLen_HK
dc.contributor.authorHu, Jen_HK
dc.date.accessioned2007-09-12T03:51:28Z-
dc.date.available2007-09-12T03:51:28Z-
dc.date.issued1997en_HK
dc.identifierhttp://hmg.oxfordjournals.org/cgi/reprint/6/12/2117en_HK
dc.identifier.citationHuman Molecular Genetics, 1997, v. 6 n. 12, p. 2117-2126en_HK
dc.identifier.issn0964-6906en_HK
dc.identifier.urihttp://hdl.handle.net/10722/44327-
dc.description.abstractNuclear RNA splicing occurs in an RNA-protein complex, termed the spliceosome. U4/U6 snRNP is one of four essential small nuclear ribonucleoprotein (snRNP) particles (U1, U2, U5 and U4/U6) present in the spliceosome. U4/U6 snRNP contains two snRNAs (U4 and U6) and a number of proteins. We report here the identification and characterization of two human genes encoding U4/U6-associated splicing factors, Hprp3p and Hprp4p, respectively. Hprp3p is a 77 kDa protein, which is homologous to the Saccharomyces cerevisiae splicing factor Prp3p. Amino acid sequence analysis revealed two putative homologues in Caenorhabditis elegans and Schizosaccharomyces pombe. Polyclonal antibodies against Hprp3p were generated with His-tagged Hprp3p over-produced in Escherichia coli. This splicing factor can co-immunoprecipitate with U4, U6 and U5 snRNAs, suggesting that it is present in the U4/U6 U5 tri-snRNP. Hprp4p is a 58 kDa protein homologous to yeast splicing factor Prp4p. Like yeast Prp4p, the human homologue contains repeats homologous to the β-subunit of G-proteins. These repeats are called WD repeats because there is a highly conserved dipeptide of tryptophan and aspartic acid present at the end of each repeat. The primary amino acid sequence homology between human Hprp4p and yeast Prp4p led to the discovery of two additional WD repeats in yeast Prp4p. Structural homology between these human and yeast splicing factors and the β-subunit of G-proteins has been identified by sequence-similarity comparison and analysis of the protein folding by threading. Structural models of Hprp4p and Prp4p with a seven-blade β-propeller topology have been generated based on the structure of β-transducin. Hprp3p and Hprp4p have been shown to interact with each other and the first 100 amino acids of Hprp3p are not essential for this interaction. These experiments suggest that both Hprp3p and Hprp4p are components of human spliceosomes.en_HK
dc.languageengen_HK
dc.publisherOxford University Press. The Journal's web site is located at http://hmg.oxfordjournals.org/en_HK
dc.relation.ispartofHuman Molecular Geneticsen_HK
dc.subject.meshImmunoblottingen_HK
dc.subject.meshNuclear proteins - genetics - metabolismen_HK
dc.subject.meshProtein-serine-threonine kinases - genetics - metabolismen_HK
dc.subject.meshSaccharomyces cerevisiae proteinsen_HK
dc.subject.meshSchizosaccharomyces pombe proteinsen_HK
dc.titleIdentification and characterization of human genes encoding Hprp3p and Hprp4p, interacting components of the spliceosomeen_HK
dc.typeArticleen_HK
dc.identifier.emailTsui, LC: tsuilc@hkucc.hku.hken_HK
dc.identifier.authorityTsui, LC=rp00058en_HK
dc.description.naturelink_to_OA_fulltexten_HK
dc.identifier.doi10.1093/hmg/6.12.2117en_HK
dc.identifier.pmid9328476-
dc.identifier.scopuseid_2-s2.0-9844236474en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-9844236474&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume6en_HK
dc.identifier.issue12en_HK
dc.identifier.spage2117en_HK
dc.identifier.epage2126en_HK
dc.identifier.isiWOS:A1997YF21200015-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWang, A=7404620105en_HK
dc.identifier.scopusauthoridFormanKay, J=7005096957en_HK
dc.identifier.scopusauthoridLuo, Y=55187937500en_HK
dc.identifier.scopusauthoridLuo, M=7202891707en_HK
dc.identifier.scopusauthoridChow, YH=7202906132en_HK
dc.identifier.scopusauthoridPlumb, J=7006808946en_HK
dc.identifier.scopusauthoridFriesen, JD=7005272510en_HK
dc.identifier.scopusauthoridTsui, LC=7102754167en_HK
dc.identifier.scopusauthoridHeng, HHQ=7005338076en_HK
dc.identifier.scopusauthoridWoolford Jr, JL=7003694172en_HK
dc.identifier.scopusauthoridHu, J=7406420553en_HK

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