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Related Experiment Videos

ATRIP associates with replication protein A-coated ssDNA through multiple interactions.

Yuka Namiki1, Lee Zou

  • 1Massachusetts General Hospital Cancer Center, Charlestown, MA 02129, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 13, 2006
PubMed
Summary

The ATM- and rad3-related (ATR)-interacting protein (ATRIP) binds to DNA damage structures via multiple interactions with replication protein A (RPA)-ssDNA. These redundant binding mechanisms ensure ATR-ATRIP complex recruitment for DNA repair.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Genetics

Background:

  • The ATM- and rad3-related (ATR)-mediated checkpoint pathway is vital for cellular responses to DNA damage and replication stress.
  • ATR-interacting protein (ATRIP) partners with ATR, binding to replication protein A (RPA)-coated single-stranded DNA (ssDNA) to facilitate ATR-ATRIP complex recognition of DNA damage structures.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying the association between ATRIP and RPA-ssDNA.
  • To identify specific domains within ATRIP responsible for RPA-ssDNA binding and understand the nature of these interactions.

Main Methods:

  • Site-directed mutagenesis of ATRIP to create mutants lacking specific domains.
  • Biochemical assays to assess the binding affinity of ATRIP and its mutants to RPA-ssDNA.

Related Experiment Videos

  • Analysis of ATRIP-RPA-ssDNA complex formation.

    • Main Results:

    • ATRIP associates with RPA-ssDNA through multiple interaction sites.
    • Two primary RPA-ssDNA-interacting domains were mapped to regions flanking ATRIP's coiled-coil domain.
    • ATRIP mutants lacking the N terminus retained RPA-ssDNA binding ability, suggesting redundant interaction mechanisms.
    • An internal ATRIP region showed affinity for ssDNA, and the N terminus exhibited dual binding modes to RPA-ssDNA.

    Conclusions:

    • The association between ATRIP and RPA-ssDNA is complex and involves multiple, potentially redundant, interactions.
    • These findings highlight a dynamic and regulated binding mechanism critical for ATR-ATRIP complex recruitment to DNA damage sites.
    • ATRIP's direct interaction with ssDNA adds another layer to understanding DNA damage recognition.