Recognition of cap structure in splicing in vitro of mRNA precursors

@article{Konarska1984RecognitionOC,
  title={Recognition of cap structure in splicing in vitro of mRNA precursors},
  author={Maria M. Konarska and Richard A. Padgett and Phillip A. Sharp},
  journal={Cell},
  year={1984},
  volume={38},
  pages={731-736}
}

Role of Eukaryotic Messenger RNA Cap-Binding Protein in Regulation of Translation

Recent in vitro studies have demonstrated that nuclear events such as mRNA splicing and 3′-end processing are more efficient when the transcripts possess a 5′ cap structure, and capped mRNAs are stabilized against 5′ exonucleolytic degradation.

The multifaceted eukaryotic cap structure

Recent findings concerning the cap epitranscriptome, the understanding of cap binding by different CBPs, and therapeutic targeting of CBP‐cap interaction are focused on.

A cap binding protein that may mediate nuclear export of RNA polymerase II-transcribed RNAs

A CBP, whose specificity for different analogs correlates with the ability of the analogs to inhibit U1 snRNA export, is identified in nuclear extracts prepared from HeLa cells and it is proposed that this protein may have a role in the export of capped RNAs from the nucleus.

Isolation and analysis of splicing complexes.

A cap-binding protein complex mediating U snRNA export

It is demonstrated that CBC mediates the effect of the cap structure in U snRNA export, and direct evidence for the involvement of a cellular RNA-binding factor in the transport of RNA to the cytoplasm is provided.

In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules.

  • A. A. HallerP. Sarnow
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1997
The cap-binding RNA specifically inhibited the translation of capped but not uncapped mRNA molecules in cell-free lysates prepared from either human HeLa cells or from Saccharomyces cerevisiae.

5'-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II.

Results suggest that Pol II-specific capping of nascent transcripts in vivo is enhanced by recruitment of the capping enzymes to the CTD and capping is co-ordinated with CTD phosphorylation.

Yeast mRNA splicing in vitro.

A nuclear cap-binding complex facilitates association of U1 snRNP with the cap-proximal 5' splice site.

It is demonstrated that CBC is required for efficient recognition of the 5' splice site by U1 snRNP during formation of E (early) complex on a pre-mRNA containing a single intron, and this function is conserved in humans and yeast.
...

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A soluble whole-cell extract prepared accurately from HeLa cells splices 2-3% of the RNA transcribed from a DNA template containing the first and second leader exons of late adenovirus RNA. The

Importance of 5'-terminal blocking structure to stabilize mRNA in eukaryotic protein synthesis.

Results show that one of the confronting nucleotide structure's functions is to stabilize the mRNA, to prevent its degradation, and that this function is important for protein synthesis in a wheat germ cell-free system.