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Enzyme
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Target Concepts:
Gene/Protein
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Query: UNIPROT:P17931 (
galectin-3
)
2,860
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Previously, we showed that galectin-1 and
galectin-3
are redundant pre-mRNA splicing factors associated with the spliceosome throughout the splicing pathway. Here we present evidence for the association of
galectin-3
with snRNPs outside of the spliceosome (i.e., in the absence of pre-mRNA splicing substrate). Immunoprecipitation of HeLa nuclear extract with anti-
galectin-3
resulted in the coprecipitation of the five spliceosomal snRNAs, core Sm polypeptides, and the U1-specific protein, U1 70K. When nuclear extract was fractionated on glycerol gradients, some
galectin-3
molecules cosedimented with snRNP complexes. This cosedimentation represents bona fide
galectin-3
--snRNP complexes as (i) immunoprecipitation of gradient fractions with anti-
galectin-3
yielded several complexes with varying ratios of snRNAs and associated proteins and (ii) the distribution of
galectin-3
--snRNP complexes was altered when the glycerol gradient was sedimented in the presence of lactose, a galectin ligand. A complex at approximately 10S showed an association of
galectin-3
with U1 snRNP that was sensitive to treatment with ribonuclease A. We tested the ability of this U1 snRNP to recognize an exogenous pre-mRNA substrate. Under conditions that assemble early splicing complexes, we found this isolated
galectin-3
--U1 snRNP particle was sufficient to load
galectin-3
onto a pre-mRNA substrate, but not onto a control RNA lacking splice sites. Pretreatment of the U1 snRNP with
micrococcal nuclease
abolished the assembly of
galectin-3
onto this early complex. These data identify
galectin-3
as a polypeptide associated with snRNPs in the absence of splicing substrate and describe a mechanism for the assembly of
galectin-3
onto the forming spliceosome.
...
PMID:A mechanism for incorporation of galectin-3 into the spliceosome through its association with U1 snRNP. 1960 45