170:(Crossover junction endodeoxyribonuclease RuvC) is the resolvase, which cleaves the Holliday junction. RuvC proteins have been shown to form dimers in solution and its structure has been solved at 2.5A. It is thought to bind either on the open, DNA exposed face of a single RuvA tetramer, or to replace one of the two tetramers. Binding is proposed to be mediated by an unstructured loop on RuvC, which becomes structured on binding RuvA. RuvC can be bound to the complex in either orientation, therefore resolving Holliday junctions in either a horizontal or vertical manner.
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159:(Holliday junction branch migration complex subunit RuvB) is an ATPase that is only active in the presence of DNA and compared to RuvA, RuvB has a low affinity for DNA. The RuvB proteins are thought to form hexameric rings on the exit points of the newly formed DNA duplexes, and it is proposed that they 'spool' the emerging DNA through the RuvA tetramer.
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RuvA and RuvB bind to the four strand DNA structure formed in the
Holliday junction intermediate, and migrate the strands through each other, using a putative spooling mechanism. The RuvAB complex can carry out DNA helicase activity, which helps unwind the duplex DNA. The binding of the RuvC protein
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and EM data, and suggest that the complex consists of either one or two RuvA tetramers, with charge lined grooves through which the incoming DNA is channelled. The structure also showed the presence of so-called 'acidic pins' in the centre of the tetramer, which serve to separate the DNA duplexes.
143:(Holliday junction branch migration complex subunit RuvA) is a DNA-binding protein that binds Holliday junctions with high affinity. The structure of the complex has been variously elucidated through
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Eggleston AK, Mitchell AH, and West SC (1997). “In Vitro
Reconstitution of the Late Steps of Genetic Recombination in E. coli”. Cell. 89: 607–617.
199:"RuvA - Holliday junction ATP-dependent DNA helicase RuvA - Thermus thermophilus (Strain ATCC 27634 / DSM 579 / HB8) - ruvA gene & protein"
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Kowalczykowski SC (2000). "Initiation of genetic recombination and recombination-dependent replication".
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to the RuvAB complex is thought to cleave the DNA strands, thereby resolving the
Holliday junction.
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West SC (2003). "Molecular views of recombination proteins and their control".
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The RuvABC is a complex of three proteins that resolve the
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in bacteria. As such, RuvABC is critical to bacterial
111:RuvA-RuvB complex heteromer, Thermus thermophilus
148:Its crystal structure has been solved at 1.9A.
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361:at the U.S. National Library of Medicine
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32:This article includes a list of general
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334:10.1016/S0968-0004(00)01569-3
359:Holliday+Junction+Resolvases
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363:Medical Subject Headings
285:Nat. Rev. Mol. Cell Biol
130:homologous recombination
128:formed during bacterial
98:homologous recombination
53:more precise citations.
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84:is a complex of three
145:X-ray crystallography
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322:Trends Biochem. Sci
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126:Holliday junction
94:Holliday junction
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186:References
102:DNA repair
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379:Proteins
373:Category
342:10754547
313:28474965
305:12778123
174:See also
86:proteins
265:6 April
240:6 April
47:improve
365:(MeSH)
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256:"RuvC"
231:"RuvB"
213:"RuvA"
180:RecBCD
82:RuvABC
36:, but
309:S2CID
338:PMID
301:PMID
267:2024
242:2024
168:RuvC
163:RuvC
157:RuvB
152:RuvB
141:RuvA
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