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Related Concept Videos

RNA Splicing01:32

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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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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.
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Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Most plants use the C3 pathway for carbon fixation. However, some plants, such as sugar cane, corn, and cacti that grow in hot conditions, use alternative pathways to fix carbon and conserve energy loss due to photorespiration. Photorespiration is the process that occurs when the oxygen concentration is high. Under such conditions, the rubisco enzyme in the Calvin cycle binds O2 instead of CO2, which halts photosynthesis and consumes energy.
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Updated: Jan 26, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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Off-Pathway-Sensitive Protein-Splicing Screening Based on a Toxin/Antitoxin System.

Hannes M Beyer1, Hideo Iwaï1

  • 1Research Program in Structural Biology and Biophysics, University of Helsinki, Viikinkaari 1, 00014, Helsinki, Finland.

Chembiochem : a European Journal of Chemical Biology
|April 10, 2019
PubMed
Summary

This study introduces a stringent screening method for protein splicing, linking it to cell survival. This approach effectively selects productive cis- and trans-splicing inteins, overcoming limitations of previous systems.

Keywords:
antitoxinsinteinprotein splicingselection screentoxins

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Protein-splicing domains are valuable tools for in vivo and in vitro protein ligation.
  • Directed evolution enhances protein-splicing technologies, but existing screening systems face challenges like pseudo-positive clones.

Purpose of the Study:

  • To develop a stringent screening method for identifying productive cis- and trans-protein splicing domains.
  • To overcome bottlenecks in current screening systems, such as off-pathway reactions and fragment complementation.

Main Methods:

  • Fusing splicing domains to an intrinsically disordered region of the Escherichia coli CcdA/CcdB type II toxin/antitoxin system's antidote.
  • Linking protein splicing activity directly to cellular survival.
  • Utilizing a stringent selection mechanism to isolate genuinely splicing inteins.

Main Results:

  • A novel screening method was established for both cis- and trans-protein splicing.
  • The method successfully selects for productively splicing domains, excluding false positives.
  • The screen enables the identification of novel inteins with high splicing efficiency.

Conclusions:

  • The developed screening system provides a robust platform for identifying and engineering highly efficient protein-splicing inteins.
  • This method advances the application of protein splicing in biotechnology and synthetic biology.
  • It facilitates the discovery of new inteins from directed evolution or natural libraries.