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dc.contributor.authorWu, Shaoping
dc.contributor.authorGreen, Michael R.
dc.date2022-08-11T08:10:02.000
dc.date.accessioned2022-08-23T16:52:48Z
dc.date.available2022-08-23T16:52:48Z
dc.date.issued1997-07-16
dc.date.submitted2008-07-09
dc.identifier.citation<p>EMBO J. 1997 Jul 16;16(14):4421-32. <a href="http://dx.doi.org/10.1093/emboj/16.14.4421">Link to article on publisher's site</a></p>
dc.identifier.issn0261-4189 (Print)
dc.identifier.doi10.1093/emboj/16.14.4421
dc.identifier.pmid9250686
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42127
dc.description.abstractAccurate splicing of precursor mRNAs (pre-mRNAs) requires recognition of the 5' and 3' splice sites at the intron boundaries. Interactions between several splicing factors and the 5' splice site, which occur prior to the first step of splicing, have been well described. In contrast, recognition of the 3' splice site, which is cleaved during the second catalytic step, is poorly understood, particularly in higher eukaryotes. Here, using site-specific photo-crosslinking, we find that the conserved AG dinucleotide at the 3' splice site is contacted specifically by a 70 kDa polypeptide (p70). The p70-3' splice site crosslink has kinetics and biochemical requirements similar to those of splicing, was detected only in the mature spliceosome and occurs subsequent to the first step. Thus, p70 has all the properties expected of a factor that functionally interacts with the 3' splice site during the second step of splicing. Using antisera to various known splicing factors, we find that p70 corresponds to a previously reported 69 kDa protein of unknown function associated with the Sm core domain of spliceosomal small nuclear ribonucleoproteins.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9250686&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170068/
dc.subjectCross-Linking Reagents
dc.subjectDinucleoside Phosphates
dc.subjectElectrophoresis, Gel, Two-Dimensional
dc.subjectHumans
dc.subjectImmunoblotting
dc.subjectIntrons
dc.subjectNuclear Proteins
dc.subjectPeptides
dc.subjectPrecipitin Tests
dc.subjectRNA Precursors
dc.subject*RNA Splicing
dc.subjectSpliceosomes
dc.subjectSuccinimides
dc.subjectUltraviolet Rays
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleIdentification of a human protein that recognizes the 3' splice site during the second step of pre-mRNA splicing
dc.typeArticle
dc.source.journaltitleThe EMBO journal
dc.source.volume16
dc.source.issue14
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/502
dc.identifier.contextkey544984
html.description.abstract<p>Accurate splicing of precursor mRNAs (pre-mRNAs) requires recognition of the 5' and 3' splice sites at the intron boundaries. Interactions between several splicing factors and the 5' splice site, which occur prior to the first step of splicing, have been well described. In contrast, recognition of the 3' splice site, which is cleaved during the second catalytic step, is poorly understood, particularly in higher eukaryotes. Here, using site-specific photo-crosslinking, we find that the conserved AG dinucleotide at the 3' splice site is contacted specifically by a 70 kDa polypeptide (p70). The p70-3' splice site crosslink has kinetics and biochemical requirements similar to those of splicing, was detected only in the mature spliceosome and occurs subsequent to the first step. Thus, p70 has all the properties expected of a factor that functionally interacts with the 3' splice site during the second step of splicing. Using antisera to various known splicing factors, we find that p70 corresponds to a previously reported 69 kDa protein of unknown function associated with the Sm core domain of spliceosomal small nuclear ribonucleoproteins.</p>
dc.identifier.submissionpathoapubs/502
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentHoward Hughes Medical Institute
dc.source.pages4421-32


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