A nuclear cap binding protein complex involved in pre-mRNA splicing
Abstract
A cap-binding protein complex (CBC) present in the nuclei of HeLa cells has been characterized. Purified CBC consists of two previously identified proteins, CBP80 and CBP20. These proteins are shown to cofractionate to apparent homogeneity and to be coimmunoprecipitable with anti-CBP80 antibodies. Analysis of the inhibition of pre-mRNA splicing in vitro and in vivo by chemically modified analogs of the cap structure, and of the binding of these analogs to CBC in vitro, suggests a role for the complex in splicing. Extracts immunodepleted of CBC do not efficiently splice an adenoviral pre-mRNA owing to blockage of an early step in splicing complex formation. CBC may therefore play a role in pre-mRNA recognition.
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5′-capping functions as binding site of eIF4F heterodimeric translation initiation complex.
“Screening mRNA against exonuclease activity, promoting pre-mRNA splicing, and functioning as binding site of eIF4F heterodimeric translation initiation complex are all important functions of 5′-capping (Izaurralde et al. 1994; Gallie 1991).”
From Modifications of mRNA vaccine structural elements for improving mRNA stability and translation efficiency (2022) · cites this paper as Izaurralde et al. 1994
5′-capping promotes pre-mRNA splicing.
“Screening mRNA against exonuclease activity, promoting pre-mRNA splicing, and functioning as binding site of eIF4F heterodimeric translation initiation complex are all important functions of 5′-capping (Izaurralde et al. 1994; Gallie 1991).”
From Modifications of mRNA vaccine structural elements for improving mRNA stability and translation efficiency (2022) · cites this paper as Izaurralde et al. 1994
5′-capping screens mRNA against exonuclease activity.
“Screening mRNA against exonuclease activity, promoting pre-mRNA splicing, and functioning as binding site of eIF4F heterodimeric translation initiation complex are all important functions of 5′-capping (Izaurralde et al. 1994; Gallie 1991).”
From Modifications of mRNA vaccine structural elements for improving mRNA stability and translation efficiency (2022) · cites this paper as Izaurralde et al. 1994
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- Authors
- Izaurralde, E., Lewis, J., McGuigan, C., Jankowska, M., Darzynkiewicz, E., & Mattaj, I. W.
- Affiliations
- European Molecular Biology Laboratory (DE)
- University of Warsaw (PL)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1994-08
- Volume
- 78
- Issue
- 4
- Pages
- 657-668
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2076304484
- Cited by
- 517
- References
- 0
- Citations by year
- 2026: 11 · 2025: 13 · 2024: 8 · 2023: 14 · 2022: 9 · 2021: 12 · 2020: 13 · 2019: 11 · 2018: 15 · 2017: 16 · 2016: 17 · 2015: 12 · 2014: 19 · 2013: 19 · 2012: 16
- FWCI
- 7.68
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- CBP80, CBP20, pre-mRNA splicing, mRNA cap, HeLa cells
- MeSH terms
- Amino Acid Sequence, Animals, Antibody Specificity, Cell Extracts, Cell Nucleus, Cloning, Molecular, HeLa Cells, Humans, Molecular Sequence Data, Protein Binding, Recombinant Fusion Proteins, RNA Cap Analogs, RNA Caps, RNA Precursors, RNA Splicing, Xenopus laevis, RNA-Binding Proteins, Spliceosomes, Sequence Analysis, DNA, RNA Cap-Binding Proteins
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