Abstract:
:In previous studies, we reported that fractionation of HeLa cell nuclear extracts on glycerol gradients revealed an endogenous ∼10S particle that contained galectin-3 and U1 snRNP and this particle was sufficient to load the galectin polypeptide onto a pre-mRNA substrate. We now document that this interaction between the galectin-3-U1 snRNP particle and the pre-mRNA results in a productive spliceosomal complex, leading to intermediates and products of the splicing reaction. Nuclear extracts were depleted of U1 snRNP with a concomitant loss of splicing activity. Splicing activity in the U1-depleted extract can be reconstituted by the galectin-3-U1 snRNP particle, isolated by immunoprecipitation of the 10S region (fractions 3-5) of the glycerol gradient with anti-galectin-3 antibodies. In contrast, parallel anti-galectin-3 immunoprecipitation of free galectin-3 molecules not in a complex with U1 snRNP (fraction 1 of the same gradient), failed to restore splicing activity. These results indicate that the galectin-3-U1 snRNP-pre-mRNA ternary complex is a functional E complex and that U1 snRNP is required to assemble galectin-3 onto an active spliceosome.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Haudek KC,Voss PG,Wang JL,Patterson RJdoi
10.1093/nar/gkw303subject
Has Abstractpub_date
2016-07-27 00:00:00pages
6391-7issue
13eissn
0305-1048issn
1362-4962pii
gkw303journal_volume
44pub_type
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