Show simple item record

dc.contributor.authorGaur, Rajesh K.
dc.contributor.authorValcarcel, Juan
dc.contributor.authorGreen, Michael R.
dc.date2022-08-11T08:09:35.000
dc.date.accessioned2022-08-23T16:36:25Z
dc.date.available2022-08-23T16:36:25Z
dc.date.issued1995-06-01
dc.date.submitted2009-03-31
dc.identifier.citation<p>RNA. 1995 Jun;1(4):407-17.</p>
dc.identifier.issn1355-8382 (Print)
dc.identifier.pmid7493318
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38782
dc.description.abstractSplicing of pre-mRNAs occurs via a lariat intermediate in which an intronic adenosine, embedded within a branch point sequence, forms a 2',5'-phosphodiester bond (RNA branch) with the 5' end of the intron. How the branch point is recognized and activated remains largely unknown. Using site-specific photochemical cross-linking, we have identified two proteins that specifically interact with the branch point during the splicing reaction. U2AF65, an essential splicing factor that binds to the adjacent polypyrimidine tract, crosslinks to the branch point at the earliest stage of spliceosome formation in an ATP-independent manner. A novel 28-kDa protein, which is a constituent of the mature spliceosome, contacts the branch point after the first catalytic step. Our results indicate that the branch point is sequentially recognized by distinct splicing factors in the course of the splicing reaction.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=7493318&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1482402/
dc.subjectBase Sequence
dc.subjectCross-Linking Reagents
dc.subjectMolecular Sequence Data
dc.subject*Nuclear Proteins
dc.subject*Nucleic Acid Conformation
dc.subjectProtein Binding
dc.subjectRNA Precursors
dc.subjectRNA Splicing
dc.subjectRNA, Messenger
dc.subjectRibonucleoproteins
dc.subjectSpliceosomes
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleSequential recognition of the pre-mRNA branch point by U2AF65 and a novel spliceosome-associated 28-kDa protein
dc.typeJournal Article
dc.source.journaltitleRNA (New York, N.Y.)
dc.source.volume1
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1628
dc.identifier.contextkey805449
html.description.abstract<p>Splicing of pre-mRNAs occurs via a lariat intermediate in which an intronic adenosine, embedded within a branch point sequence, forms a 2',5'-phosphodiester bond (RNA branch) with the 5' end of the intron. How the branch point is recognized and activated remains largely unknown. Using site-specific photochemical cross-linking, we have identified two proteins that specifically interact with the branch point during the splicing reaction. U2AF65, an essential splicing factor that binds to the adjacent polypyrimidine tract, crosslinks to the branch point at the earliest stage of spliceosome formation in an ATP-independent manner. A novel 28-kDa protein, which is a constituent of the mature spliceosome, contacts the branch point after the first catalytic step. Our results indicate that the branch point is sequentially recognized by distinct splicing factors in the course of the splicing reaction.</p>
dc.identifier.submissionpathoapubs/1628
dc.contributor.departmentHoward Hughes Medical Institute, Program in Molecular Medicine
dc.source.pages407-17


This item appears in the following Collection(s)

Show simple item record