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The DNA binding and pairing preferences of the archaeal RadA protein demonstrate a universal characteristic of DNA strand exchange proteins
Author(s) -
Seitz Erica M.,
Kowalczykowski Stephen C.
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.02009.x
Subject(s) - biology , sulfolobus solfataricus , dna , dna binding protein , saccharomyces cerevisiae , rad51 , genetics , escherichia coli , biochemistry , microbiology and biotechnology , gene , archaea , dna repair , transcription factor
The archaeal RadA protein is a homologue of the Escherichia coli RecA and Saccharomyces cerevisiae Rad51 proteins and possesses the same biochemical activities. Here, using in vitro selection, we show that the Sulfolobus solfataricus RadA protein displays the same preference as its homologues for binding to DNA sequences that are rich in G residues, and under‐represented in A and C residues. The RadA protein also displays enhanced pairing activity with these in vitro ‐selected sequences. These parallels between the archaeal, eukaryal and bacterial proteins further extend the universal characteristics of DNA strand exchange proteins.