Yeast DNA recombination and repair proteins Rad1 and Rad10 constitute a complex in vivo mediated by localized hydrophobic domains

A. Jane Bardwell, Lee Bardwell, Douglas K. Johnson, Errol C. Friedberg

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

The Saccharomyces cerevisiae Rad1 and Radio proteins are required for damage-specific incision during nucleotide excision repair and also for certain mitotic recombination events between repeated sequences. Previously we have demonstrated that Rad1 and Rad10 form a specific complex in vitro. Using the 'two-hybrid' genetic assay system we now report that Rad1 and Rad10 proteins are subunits of a specific complex in the cell nucleus. The Rad10-binding domain of Rad1 protein maps to a localized region between amino acids 809-997. The Rad1-binding domain of Rad10 protein maps between amino acids 90-210. These domains are evolutionarily conserved and are hydrophobic in character. Although significant homology exists between Rad10 and the human-DNA-repair protein Ercc1 in this region, we were unable to detect any interaction between Ercc1 and Rad1 proteins. We conclude that Rad1 and Rad10 operate in DNA repair and mitotic recombination as a constitutive complex.

Original languageEnglish (US)
Pages (from-to)1177-1188
Number of pages12
JournalMolecular Microbiology
Volume8
Issue number6
StatePublished - Jun 1993

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Recombinational DNA Repair
DNA Repair
Yeasts
Genetic Recombination
Amino Acids
Two-Hybrid System Techniques
Proteins
Protein Subunits
Cell Nucleus
Radio
Saccharomyces cerevisiae
Protein Domains

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Yeast DNA recombination and repair proteins Rad1 and Rad10 constitute a complex in vivo mediated by localized hydrophobic domains. / Bardwell, A. Jane; Bardwell, Lee; Johnson, Douglas K.; Friedberg, Errol C.

In: Molecular Microbiology, Vol. 8, No. 6, 06.1993, p. 1177-1188.

Research output: Contribution to journalArticle

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