TY - JOUR
T1 - The DNA binding and pairing preferences of the archaeal RadA protein demonstrate a universal characteristic of DNA strand exchange proteins
AU - Seitz, Erica M.
AU - Kowalczykowski, Stephen C.
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
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U2 - 10.1046/j.1365-2958.2000.02009.x
DO - 10.1046/j.1365-2958.2000.02009.x
M3 - Article
C2 - 10931349
AN - SCOPUS:0033867763
VL - 37
SP - 555
EP - 560
JO - Molecular Microbiology
JF - Molecular Microbiology
SN - 0950-382X
IS - 3
ER -