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RNA Splicing01:32

RNA Splicing

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Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...
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Pre-mRNA Processing: RNA Splicing01:36

Pre-mRNA Processing: RNA Splicing

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Alternative RNA Splicing02:18

Alternative RNA Splicing

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Alternative RNA splicing is the regulated splicing of exons and introns to produce different mature mRNAs from a single pre-mRNA. Unlike in constitutive splicing where a single gene produces a single type of mRNA, alternative splicing allows an organism to produce multiple proteins from a single gene and plays an important role in protein diversity.
There are five types of alternative RNA splicing that vary in the ways the pre-mRNA segments are removed or retained in the mature mRNA. The first...
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Alternative RNA Splicing02:18

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Chromatin Structure and RNA Splicing02:41

Chromatin Structure and RNA Splicing

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Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

Pre-mRNA Processing: Modification of pre-mRNA Ends

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In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps...
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Related Experiment Video

Updated: Dec 13, 2025

A Reporter Based Cellular Assay for Monitoring Splicing Efficiency
08:53

A Reporter Based Cellular Assay for Monitoring Splicing Efficiency

Published on: September 15, 2021

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SHAPE Profiling to Probe Group II Intron Conformational Dynamics During Splicing.

Timothy Wiryaman1, Navtej Toor2

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|July 27, 2020
PubMed
Summary

Selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE) and mutational profiling (SHAPE-MaP) reveal RNA conformational changes. This study applies SHAPE-MaP to track group II intron self-splicing dynamics.

Keywords:
Chemical structure probingGroup II intronNext-generation sequencingRNA structureSHAPE-MaP

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • RNA Biology

Background:

  • Selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE) is a key method for RNA structure analysis.
  • SHAPE probes nucleotide flexibility within local RNA structures.
  • Understanding RNA conformational dynamics is crucial for deciphering biological functions.

Purpose of the Study:

  • To apply SHAPE-MaP (mutational profiling) to investigate RNA conformational states.
  • To analyze the dynamic structural changes of group II introns during self-splicing.

Main Methods:

  • Utilized SHAPE-MaP, a technique combining SHAPE with mutational profiling.
  • Applied the method to study the group II intron self-splicing reaction.
  • Characterized nucleotide flexibility and conformational transitions.

Main Results:

  • Demonstrated the utility of SHAPE-MaP in capturing distinct conformational states of the group II intron.
  • Provided insights into the structural rearrangements occurring during the self-splicing process.
  • Mapped nucleotide flexibility changes correlated with splicing progression.

Conclusions:

  • SHAPE-MaP is a powerful tool for dissecting RNA conformational dynamics in complex biological processes.
  • The study elucidates the structural basis of group II intron self-splicing.
  • This approach advances the understanding of RNA structure-function relationships.