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Related Concept Videos

DNA Helicases00:55

DNA Helicases

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DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
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Nucleosome Remodeling02:54

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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Mismatch Repair01:36

Mismatch Repair

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Overview
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Mismatch Repair01:20

Mismatch Repair

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Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
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The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
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Related Experiment Video

Updated: Apr 14, 2026

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks
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Genome Protection by the 9-1-1 Complex Subunit HUS1 Requires Clamp Formation, DNA Contacts, and ATR

Pei Xin Lim1, Darshil R Patel1, Kelsey E Poisson1

  • 1From the Department of Biomedical Sciences, Cornell University, Ithaca, New York 14853 and.

The Journal of Biological Chemistry
|April 26, 2015
PubMed
Summary

The RAD9A-HUS1-RAD1 (9-1-1) complex is crucial for DNA repair. This study identified key HUS1 residues essential for its assembly, DNA binding, and recruitment of repair proteins, ensuring genome stability.

Keywords:
DNA damage, DNA damage response, checkpoint control, proliferating cell nuclear antigen (PCNA), genomic instability, HUS1, 9-1-1 complex

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Related Experiment Videos

Last Updated: Apr 14, 2026

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • The RAD9A-HUS1-RAD1 (9-1-1) complex functions as a sliding clamp at DNA damage sites.
  • It plays a critical role in activating checkpoint signaling and DNA repair pathways.

Purpose of the Study:

  • To identify specific functional residues within the HUS1 protein.
  • To understand how these residues contribute to 9-1-1 complex assembly, DNA interaction, and effector functions.

Main Methods:

  • Site-directed mutagenesis to alter HUS1 residues.
  • Assays for complex assembly and DNA loading.
  • Analysis of chromatin localization and signaling pathways (ATR, CHK1).
  • Cell survival assays post-genotoxin exposure.

Main Results:

  • A HUS1-RAD9A interface residue is critical for 9-1-1 complex assembly and DNA loading.
  • Positively charged residues in HUS1's inner ring are essential for DNA damage-induced chromatin localization and ATR signaling.
  • Hydrophobic pockets on HUS1's outer surface are vital for cell survival but not for chromatin loading or CHK1 activation, mediating interactions with MYH.

Conclusions:

  • The 9-1-1 complex performs distinct functions at DNA damage sites.
  • Specific HUS1 residues dictate clamp assembly, DNA binding, and recruitment of downstream effectors.
  • These findings provide insights into genome maintenance mechanisms.