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Related Experiment Videos

Conserved structure for single-stranded telomeric DNA recognition.

Rachel M Mitton-Fry1, Emily M Anderson, Timothy R Hughes

  • 1Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.

Science (New York, N.Y.)
|April 6, 2002
PubMed
Summary
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Spontaneous replication fork collapse regulates telomere length homeostasis in wild type yeast.

bioRxiv : the preprint server for biology·2026

The Cdc13 protein protects yeast chromosome ends using a unique OB fold for DNA binding. This structure reveals conserved eukaryotic mechanisms for telomere maintenance.

Area of Science:

  • Molecular Biology
  • Genetics
  • Structural Biology

Background:

  • Cdc13 is essential for chromosome end protection and telomere replication in Saccharomyces cerevisiae.
  • It functions as a single-stranded telomeric DNA binding protein.

Purpose of the Study:

  • To determine the solution structure of the Cdc13 DNA binding domain in complex with telomeric DNA.
  • To elucidate the molecular mechanisms of telomeric DNA recognition by Cdc13.

Main Methods:

  • Solution structure determination
  • X-ray crystallography
  • Biochemical assays

Main Results:

  • The structure reveals Cdc13 utilizes a single OB fold with an extended loop for DNA recognition.

Related Experiment Videos

  • The OB fold shows structural similarity to telomere end-binding proteins in other eukaryotes, despite lacking sequence similarity.
  • This highlights a conserved structural motif for telomeric DNA binding across eukaryotes.

    • Conclusions:

    • The OB fold is a conserved structural element for eukaryotic telomeric DNA binding.
    • Cdc13 employs a unique structural adaptation for efficient telomere end protection.
    • Understanding Cdc13 structure provides insights into fundamental mechanisms of genome stability.