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Literature summary extracted from

  • Khanduja, J.S.; Tripathi, P.; Muniyappa, K.
    Mycobacterium tuberculosis RuvA induces two distinct types of structural distortions between the homologous and heterologous Holliday junctions (2009), Biochemistry, 48, 27-40.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.21.10 expressed in Escherichia coli strain Origami (DE3)pLysS Mycobacterium tuberculosis

General Stability

EC Number General Stability Organism
3.1.21.10 the tetrameric RuvA-Holliday junction complex II is stable in the presence of 750 mM NaCl, whereas the same amount of salt induces more than 80% dissociation of the octameric complex I Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.21.10 Ca2+ binding of two tetramers of RuvA on the junction is favored by divalent cations, Ca2+ enhances the binding of RuvA to the junction Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.21.10 22000
-
SDS-PAGE Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.1.21.10 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.21.10 DEAE-cellulose column chromatography, ammonium sulfate fractionation, Superdex-200 gel filtration, phosphocellulose column chromatography, and hydroxyapatite Bio-Gel HTP column chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.10 Holliday junction in DNA + H2O RuvA protein binds Holliday junctions in preference to any other substrate Mycobacterium tuberculosis ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.21.10 RuvA RuvA is a Holliday junction-specific DNA-binding protein and facilitates the interaction of RuvB with the junction Mycobacterium tuberculosis