The product is a recombinant protein abundantly expressed by E. coli and purified by methods such as chromatography. The molecular weight is 22 kD and even in solution, it binds to the Holliday structure and form a tetramer.
Spezies: E. coli
Wirt: Escherichia coli (E. coli)
Native
Func
Active
Applikationshinweise
1) Functional as Holliday junction specific binding protein,which promotes Holliday-junction branch migration in combination with RuvB protein. 2) For SNP analysis (Genome Research 13:1754-1764 PMID: 12840050).
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
2.7 mg/mL
Buffer
50 % glycerol, 10 mM Tris-HCl ( pH 7.5), 2 mM EDTA, 100 mM NaCl, 5 mM mercaptoethanol
Lagerung
-20 °C
Han, Tani, Hayashi, Hishida, Iwasaki, Shinagawa, Harada: "Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, Issue 31, pp. 11544-8, (2006) (PubMed).
Iwasaki, Takahagi, Nakata, Shinagawa: "Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration." in: Genes & development, Vol. 6, Issue 11, pp. 2214-20, (1992) (PubMed).
E. coli RuvA protein binds specifically to the Holliday structure which is the intermediate of recombination at the late stage of homologous recombination and recombination repair and forms a complex with RuvB motor protein allowing the migration of Holliday junction using ATP hydrolysis energy and expands the heteroduplex region. In solution, it forms a tetramer and binds to the cross-like DNA of the Holliday junction from below and above holding it in between.