Cloning of the large subunit of replication protein A (RPA) from yeast Saccharomyces cerevisiae and its DNA binding activity through redox potential

Haeng Soon Jeong, In Chel Jeong, Andre Kim, Shin Won Kang, Sung Kang Ho, Yung Jin Kim, Suk Hee Lee, Jang Su Park

Research output: Contribution to journalArticle

6 Scopus citations


Eukaryotic replication protein A (RPA) is a single-stranded( ss) DNA binding protein with multiple functions in DNA replication, repair, and genetic recombination. The 70-kDa subunit of eukaryotic RPA contains a conserved four cysteine-type zinc-finger motif that has been implicated in the regulation of DNA replication and repair. Recently, we described a novel function for the zinc-finger motif in the regulation of human RPA's ssDNA binding activity through reduction-oxidation (redox). Here, we show that yeast RPA's ssDNA binding activity is regulated by redox potential through its RPA32 and/or RPA14 subunits. Yeast RPA requires a reducing agent, such as dithiothreitol (DTT), for its ssDNA binding activity. Also, under non-reducing conditions, its DNA binding activity decreases 20 fold. In contrast, the RPA70 subunit does not require DTT for its DNA binding activity and is not affected by the redox condition. These results suggest that all three subunits are required for the regulation of RPA's DNA binding activity through redox potential.

Original languageEnglish (US)
Pages (from-to)194-198
Number of pages5
JournalJournal of Biochemistry and Molecular Biology
Issue number2
StatePublished - Mar 1 2002



  • Redox
  • Replication protein A (RPA)
  • RPA70
  • Single-stranded DNA binding protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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