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Related Experiment Videos

Structural basis for telomeric single-stranded DNA recognition by yeast Cdc13.

Rachel M Mitton-Fry1, Emily M Anderson, Douglas L Theobald

  • 1Department of Chemistry and Biochemistry, University of Colorado, UCB 215, Boulder, CO 80309-0215 USA.

Journal of Molecular Biology
|April 7, 2004
PubMed
Summary
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The budding yeast Cdc13 protein binds telomeric single-stranded DNA (ssDNA) to protect chromosome ends. Its structure reveals a unique binding mechanism involving conserved residues and a critical beta2-beta3 loop for high-affinity, specific recognition.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Yeast Genetics

Background:

  • Telomeres protect chromosome ends from degradation and fusion.
  • Cdc13 is an essential budding yeast protein that binds telomeric single-stranded DNA (ssDNA).
  • Cdc13 utilizes an OB-fold domain for high-affinity binding to telomeric 3' overhangs.

Purpose of the Study:

  • To determine the high-resolution solution structure of the Cdc13 DNA-binding domain (DBD) complexed with telomeric ssDNA.
  • To elucidate the molecular mechanisms underlying Cdc13's specific and high-affinity binding to telomeric ssDNA.
  • To provide a structural basis for understanding telomere end protection in budding yeast.

Main Methods:

  • High-resolution solution structure determination of the Cdc13-DBD/ssDNA complex.

Related Experiment Videos

  • Analysis of protein-DNA interactions, including amino acid residue contributions and conserved elements.
  • Comparative analysis with other telomere-binding protein complexes.

    • Main Results:

    • The ssDNA wraps around the Cdc13-DBD OB-fold in an extended, irregular conformation.
    • Aromatic, basic, and hydrophobic residues, many conserved, are key for ssDNA recognition and binding energetics.
    • A unique, ordered beta2-beta3 loop is crucial for complex formation, contacting five ssDNA nucleotides.

    Conclusions:

    • Cdc13 recognizes GT-rich telomeric ssDNA sequences with high affinity and specificity through a unique binding mode.
    • The structure suggests a folding-type mechanism for recognizing extended ssDNA, differing from specific hydrogen bond patterns.
    • This structural insight is foundational for understanding telomere maintenance and end protection in budding yeast.