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Related Concept Videos

Nonsense-mediated mRNA Decay02:27

Nonsense-mediated mRNA Decay

The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
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Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...

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Related Experiment Video

Updated: May 16, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

Snm1B interacts with PSF2.

Jay R Stringer1, Christopher M Counter

  • 1Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina, United States of America.

Plos One
|November 29, 2012
PubMed
Summary
This summary is machine-generated.

The protein Snm1B interacts with PSF2, crucial for interstrand crosslink (ICL) repair. This interaction involves distinct regions of Snm1B, influencing its association with chromatin and repair complexes like Mus81.

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Last Updated: May 16, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

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Published on: March 3, 2015

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Published on: February 10, 2022

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12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Area of Science:

  • Molecular Biology
  • DNA Repair Mechanisms

Background:

  • Snm1B is vital for interstrand crosslink (ICL) repair.
  • PSF2, a GINS complex member, also participates in ICL repair.

Purpose of the Study:

  • To investigate the interaction between Snm1B and PSF2.
  • To elucidate the functional domains of Snm1B in ICL repair and chromatin association.

Main Methods:

  • Yeast two-hybrid screening to identify protein interactions.
  • Co-immunoprecipitation assays to study protein complex formation.
  • Analysis of protein domain deletions to assess functional roles.

Main Results:

  • PSF2 binds Snm1B via its N-terminal (144 aa) and C-terminal (37 aa) regions.
  • The Snm1B N-terminus is critical for recruiting Mus81 to the repair complex.
  • The Snm1B C-terminus mediates PSF2-dependent chromatin association, competing with TRF2.

Conclusions:

  • Snm1B utilizes distinct domains for interaction with PSF2, Mus81, and chromatin.
  • The N-terminal interaction with PSF2/Mus81 is key for DNA repair complex formation.
  • The C-terminal interaction with PSF2 is essential for recruiting Snm1B to chromatin during ICL repair.