RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro. | Zendy

Irina R. Tsaneva | Zendy; Berndt Müller | Zendy; Stephen C. West | Zendy

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RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro.

Author(s) -

Irina R. Tsaneva,

Berndt Müller,

Stephen C. West

Publication year - 1993

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.90.4.1315

Subject(s) - holliday junction , branch migration , helicase , dna , biology , dna repair , homologous recombination , heteroduplex , genetic recombination , microbiology and biotechnology , genetics , biophysics , gene , recombination , rna

The SOS-inducible ruvA and ruvB gene products of Escherichia coli are required for normal levels of genetic recombination and DNA repair. In vitro, RuvA protein interacts specifically with Holliday junctions and, together with RuvB (an ATPase), promotes their movement along DNA. This process, known as branch migration, is important for the formation of heteroduplex DNA. In this paper, we show that the RuvA and RuvB proteins promote the unwinding of partially duplex DNA. Using single-stranded circular DNA substrates with annealed fragments (52-558 nucleotides in length), we show that RuvA and RuvB promote strand displacement with a 5'-->3' polarity. The reaction is ATP-dependent and its efficiency is inversely related to the length of the duplex DNA. These results show that the ruvA and ruvB genes encode a DNA helicase that specifically recognizes Holliday junctions and promotes branch migration.

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