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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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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.
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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Conditional protein splicing triggered by SUMO protease.

Minghui Xu1, Suyang Wang1, Qin Zhan1

  • 1College of Biological Science and Medical Engineering, Donghua University, Shanghai, 201620, PR China.

Biochemical and Biophysical Research Communications
|March 16, 2023
PubMed
Summary
This summary is machine-generated.

We developed a new method for controlling protein activity using conditional protein splicing. A SUMO protease triggers splicing of a split intein, enabling precise control over protein function in vitro.

Keywords:
Conditional protein splicingSUMO ProteaseSplit intein

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Protein Engineering

Background:

  • Conditional protein splicing offers precise post-translational control of protein activity.
  • Split inteins are key components in protein trans-splicing systems.
  • Existing methods for controlling split intein activity have limitations.

Purpose of the Study:

  • To develop a novel conditional protein splicing system.
  • To engineer an atypical split intein responsive to SUMO protease.
  • To demonstrate SUMO protease-induced protein trans-splicing in vitro.

Main Methods:

  • Engineered the Ter DnaE-3 S11 split intein with a small C-intein segment.
  • Fused a SUMO tag to the N-terminus of the C-intein to inhibit splicing.
  • Utilized SUMO protease to induce protein trans-splicing.
  • Detected splicing products via western blotting.

Main Results:

  • SUMO protease addition triggered protein trans-splicing within 15 minutes.
  • Splicing efficiency was approximately 4-fold higher with SUMO protease compared to controls.
  • The system demonstrated effectiveness with different exteins in vitro.

Conclusions:

  • A novel SUMO protease-inducible conditional protein splicing system was established.
  • This engineered split intein provides a powerful tool for in vitro protein engineering.
  • The system offers new insights into regulating protein splicing for controlled protein function.