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dc.contributor.authorShen, Haihong
dc.contributor.authorKan, Julie L. C.
dc.contributor.authorGreen, Michael R.
dc.date2022-08-11T08:10:15.000
dc.date.accessioned2022-08-23T17:01:06Z
dc.date.available2022-08-23T17:01:06Z
dc.date.issued2004-02-18
dc.date.submitted2011-04-19
dc.identifier.citationMol Cell. 2004 Feb 13;13(3):367-76.
dc.identifier.issn1097-2765 (Linking)
dc.identifier.pmid14967144
dc.identifier.urihttp://hdl.handle.net/20.500.14038/43934
dc.description.abstractExonic splicing enhancers (ESEs) are required for splicing of certain pre-mRNAs and function by providing binding sites for serine-arginine (SR) proteins, which contain an arginine-serine-rich (RS) domain. How an RS domain bound at the ESE promotes splicing is poorly understood. We have developed an RNA-protein crosslinking procedure to identify the target of the ESE-bound RS domain. Using this approach, we show that the ESE-bound RS domain specifically contacts the pre-mRNA branchpoint. The interaction between the ESE-bound RS domain and the branchpoint occurs in the prespliceosome and is dependent upon the same splicing signals, biochemical factors, and reaction conditions required to support prespliceosome assembly. Analysis of RS domain mutants demonstrates that the ability to interact with the branchpoint, to promote prespliceosome assembly, and to support splicing are related activities. We conclude that the ESE-bound RS domain functions by contacting the branchpoint to promote prespliceosome assembly.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=14967144&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/S1097-2765(04)00025-5
dc.subjectArginine
dc.subjectBase Sequence
dc.subjectBinding Sites
dc.subjectEnhancer Elements, Genetic
dc.subjectHela Cells
dc.subjectHumans
dc.subjectMolecular Sequence Data
dc.subjectProtein Binding
dc.subjectProtein Structure, Tertiary
dc.subjectRNA Splicing
dc.subjectRNA, Messenger
dc.subjectRNA-Binding Proteins
dc.subjectRecombinant Fusion Proteins
dc.subjectSerine
dc.subjectSpliceosomes
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectGenetics and Genomics
dc.titleArginine-serine-rich domains bound at splicing enhancers contact the branchpoint to promote prespliceosome assembly
dc.typeJournal Article
dc.source.journaltitleMolecular cell
dc.source.volume13
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/pgfe_pp/146
dc.identifier.contextkey1946801
html.description.abstract<p>Exonic splicing enhancers (ESEs) are required for splicing of certain pre-mRNAs and function by providing binding sites for serine-arginine (SR) proteins, which contain an arginine-serine-rich (RS) domain. How an RS domain bound at the ESE promotes splicing is poorly understood. We have developed an RNA-protein crosslinking procedure to identify the target of the ESE-bound RS domain. Using this approach, we show that the ESE-bound RS domain specifically contacts the pre-mRNA branchpoint. The interaction between the ESE-bound RS domain and the branchpoint occurs in the prespliceosome and is dependent upon the same splicing signals, biochemical factors, and reaction conditions required to support prespliceosome assembly. Analysis of RS domain mutants demonstrates that the ability to interact with the branchpoint, to promote prespliceosome assembly, and to support splicing are related activities. We conclude that the ESE-bound RS domain functions by contacting the branchpoint to promote prespliceosome assembly.</p>
dc.identifier.submissionpathpgfe_pp/146
dc.contributor.departmentProgram in Gene Function and Expression
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages367-76


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