Atomic structure of the RuvC resolvase: A holliday junction-specific endonuclease from E. coli

Ariyoshi, Mariko; Vassylyev, Dmitry G.; Iwasaki, Hiroshi; Nakamura, Haruki; Shinagawa, Hideo; Morikawa, Kosuke

doi:10.1016/0092-8674(94)90280-1

Cited by 291 publications

(298 citation statements)

References 48 publications

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“…The structure of the ASV integrase (Bujacz et al 1995; not shown) is similar to that of the HIV integrase. RNaseH (E. coli protein (Yang et al 1990) is shown; the HIV protein is similar) and E. coli RuvC endonuclease (Ariyoshi et al 1994) also share the arrangement of the central mixed b sheet and several a helices surrounding it. The active site acidic residues are highlighted in pink.…”

Section: K Mizuuchimentioning

confidence: 99%

Polynucleotidyl transfer reactions in site‐specific DNA recombination

1997

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Site-specific DNA rearrangement reactions are widespread among organisms. They are used, for example, by vertebrates to boost immune response diversity, and in turn by parasitic organisms to evade the host immune system by surface antigen switching. Parasitic genetic elements ubiquitous to most organisms invade new host genomic sites by a variety of types of site-specific recombination. Polynucleotidyl transfer reactions are central to these DNA recombination reactions. The recombinase of each reaction system that 'catalyses' such chemical reactions at specific DNA sites are apparently designed to accomplish unique DNA geometrical specificity, or delicate control over the extent or direction of the reaction, with the sacrifice of protein turnover. Here we discuss our current understanding of several issues that relate to the polynucleotidyl transfer steps in several of the better studied site-specific recombination reactions.

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Section: K Mizuuchimentioning

confidence: 99%

Polynucleotidyl transfer reactions in site‐specific DNA recombination

1997

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“…Therefore, we concluded that L78P exists as a monomer and that this is due to a defect in dimer formation. Leu-78 is involved in the dimer interaction together with several other residues on the second ␣-helix (Ariyoshi et al 1994; see Fig. 7).…”

Section: Physical Properties Of the Mutant Ruvc Proteins In Solutionmentioning

confidence: 99%

“…In the crystal structure, RuvC forms a dimer via intersubunit interactions, mainly between the ␣B helices consisting of residues 76-93, which are arranged roughly parallel to the dyad axis in the dimer (Ariyoshi et al 1994; Fig. 7).…”

Section: Dimer Interfacementioning

confidence: 99%

“…The remainder have alterations that may disrupt hydrophobic interactions and that may affect the secondary and tertiary structures of RuvC. (Ariyoshi et al 1994). The figure was drawn using QUANTA.…”

Section: Mutations That Affect the Structurementioning

confidence: 99%

“…Crystallographic studies have revealed a three-dimensional structure of RuvC at atomic resolutions (Ariyoshi et al 1994). It forms a dimer which is related by a dyad axis.…”

Section: Introductionmentioning

confidence: 99%

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Mutational analysis on structure–function relationship of a Holliday junction specific endonuclease RuvC

et al. 1998

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DNA recognition by structure-selective nucleases

Suck

1997

Biopolymers

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The nucleases discussed in this review show little sequence specificity but instead recognize certain structural features of their respective DNA substrates. The level of their structural selectivity ranges from simple discrimination between single‐ and double‐stranded DNA (nucleases P1 and S1), the recognition of helical parameters like groove width and flexibility (DNase I), the recognition of helical distortions caused by abasic sites (exonuclease III, HAP1), to the recognition of specialized structures like flap DNA (5′‐nucleases of eukaryotes, phages, and eubacterial DNA polymerases) and four‐way junctions (T4 endonuclease VII, RuvC). The discussion is focused on the structural basis of the recognition process. In most cases the available x‐ray structures of the nucleases and/or their DNA complexes have revealed the presence of structural motifs explaining the observed structural selectivity. © 1998 John Wiley & Sons, Inc. Biopoly 44: 405–421, 1997

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Atomic structure of the RuvC resolvase: A holliday junction-specific endonuclease from E. coli

Cited by 291 publications

References 48 publications

Polynucleotidyl transfer reactions in site‐specific DNA recombination

Polynucleotidyl transfer reactions in site‐specific DNA recombination

Mutational analysis on structure–function relationship of a Holliday junction specific endonuclease RuvC

DNA recognition by structure-selective nucleases

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