Please use this identifier to cite or link to this item: https://doi.org/10.1093/nar/25.2.354
DC FieldValue
dc.titleAssociation of U2 snRNP with the spliceosomal complex E
dc.contributor.authorHong, W.
dc.contributor.authorBennett, M.
dc.contributor.authorXiao, Y.
dc.contributor.authorKramer, R.F.
dc.contributor.authorWang, C.
dc.contributor.authorReed, R.
dc.date.accessioned2014-11-28T02:49:45Z
dc.date.available2014-11-28T02:49:45Z
dc.date.issued1997
dc.identifier.citationHong, W., Bennett, M., Xiao, Y., Kramer, R.F., Wang, C., Reed, R. (1997). Association of U2 snRNP with the spliceosomal complex E. Nucleic Acids Research 25 (2) : 354-361. ScholarBank@NUS Repository. https://doi.org/10.1093/nar/25.2.354
dc.identifier.issn03051048
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/111793
dc.description.abstractIn metazoans, the E complex is operationally defined as an ATP-independent spliceosomal complex that elutes as a single peak on a gel filtration column and can be chased into spliced products in the presence of an excess of competitor pre-mRNA. The A complex is the first ATP-dependent functional spliceosomal complex. U1 snRNP first binds tightly to the 5' splice site in the E complex and U2 snRNP first binds tightly to the branch site in the A complex. In this study, we have generated and characterized a monoclonal antibody (mAb 4G8) directed against SAP 62, a component of U2 snRNP and a subunit of the essential mammalian splicing factor SF3a. We show that this antibody is highly specific for SAP 62, detecting only SAP 62 on Western blots and immunoprecipitating only SAP 62 from nuclear extracts. The-anti-SAP 62 antibody also immunoprecipitates U2 snRNP and the A complex. Significantly, however, we find that the E complex is also efficiently immunoprecipitated by the anti-SAP 62 antibody. This antibody does not cross-react with any E complex-specific components, indicating that SAP 62 itself is associated with the E complex. To determine whether other U2 snRNP components are associated with the E complex, we used antibodies to the U2 snRNP proteins B'' and SAP 155. These antibodies also specifically immunoprecipitate the E complex. These observations indicate that U2 snRNP is associated with the E complex. However, we find that U2 snRNP is not as tightly bound in the E complex as it is in the A complex. The possible significance of the weak association of U2 snRNP with the E complex is discussed.
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentINSTITUTE OF MOLECULAR & CELL BIOLOGY
dc.description.doi10.1093/nar/25.2.354
dc.description.sourcetitleNucleic Acids Research
dc.description.volume25
dc.description.issue2
dc.description.page354-361
dc.description.codenNARHA
dc.identifier.isiutA1997WD44400011
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