ArticleNucleic acids research2002
Reversible inhibition of the second step of splicing suggests a possible role of zinc in the second step of splicing.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- RNase III cleavage sites spread across splice junctions enforce sequential snoRNA processing.EMBO reports · 2025Article
- Clonal cytopenia of undetermined significance and atypical Behçet's: the importance of zinc.BMJ case reports · 2022Article
- Presynaptic dysfunction in CASK-related neurodevelopmental disorders.Translational psychiatry · 2020Article
- Physiological state co-regulates thousands of mammalian mRNA splicing events at tandem splice sites and alternative exons.Nucleic acids research · 2014Article
- Molecular architecture of zinc chelating small molecules that inhibit spliceosome assembly at an early stage.RNA (New York, N.Y.) · 2012Article
- Environmental stresses inhibit splicing in the aquatic fungus Blastocladiella emersonii.BMC microbiology · 2009Article
- Ribonucleotide reductase as one important target of [Tris(1,10-phenanthroline)lanthanum(III)] trithiocyanate (KP772).Current cancer drug targets · 2009Article
- An artificial riboswitch for controlling pre-mRNA splicing.RNA (New York, N.Y.) · 2005Article
- Splicing factor hSlu7 contains a unique functional domain required to retain the protein within the nucleus.Molecular biology of the cell · 2004Article
- The U1 snRNP base pairs with the 5' splice site within a penta-snRNP complex.Molecular and cellular biology · 2003Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A multicomponent complex of proteins and RNA is assembled on the newly synthesized pre-mRNA to form the spliceosome. This complex catalyzes a two-step transesterification reaction required to remove the introns and ligate the exons. To date, only six proteins have been found necessary for the second step of splicing in yeast, and their human homologs have been identified. We demonstrate that the addition of the selective chelator of zinc, 1,10-phenanthroline, to an in vitro mRNA splicing reaction causes a dose-dependent inhibition of the second step of splicing. This inhibition is accompanied by the accumulation of spliceosomes paused before completion of step two of the splicing reaction. The inhibition effect on the second step is due neither to snRNA degradation nor to direct binding to the mRNA, and is reversible by dialysis or add-back of zinc, but not of other divalent metals, at the beginning of the reaction. These findings suggest that the activity of a putative zinc-dependent metalloprotein(s) involved in the second step of splicing is affected. This study outlines a new method for specific reversible inhibition of the second step of splicing using external reagents, and suggests a possible role of divalent cations in the second step of mRNA splicing, most likely zinc.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.