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DNA unwinding activity of replication protein A
Author(s) -
Georgaki Anthi,
Strack Bettina,
Podust Vladimir,
Hübscher Ulrich
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81283-r
Subject(s) - dna replication , helicase , eukaryotic dna replication , replication protein a , primase , dna , pre replication complex , heterotrimeric g protein , dna clamp , replication factor c , dnaa , origin recognition complex , microbiology and biotechnology , minichromosome maintenance , replisome , chemistry , control of chromosome duplication , biology , biochemistry , dna binding protein , gene , transcription factor , rna , g protein , signal transduction , reverse transcriptase
Replication protein A (RP‐A) is a heterotrimeric complex conserved in cukaryotic cells. It binds to single‐stranded DNA and is essential for initiation and elongation of DNA replication. In this communication we give evidence that this protein can unwind DNA independent of magnesium and ATP, two essential cofactors for bona fide DNA helicase activity. RP‐A can unwind up to at least 350 basepairs and appears to be required in stoichiometric amounts. The reaction is extremely sensitive to NaCl and MgCl 2 . This activity of RF‐A is suggestive for a possible unwinding function in initiation of DNA replication in eukaryotes.