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PMID: 15093826 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Three-dimensional structural views of branch migration and resolution in DNA homologous recombination.

Current opinion in structural biology ·Vol. 14 ·No. 2 ·2004-04-00 ·Pages 130-7

Yamada K, Ariyoshi M, Morikawa K

Abstract

The processing of the Holliday junction by various proteins is a major event in DNA homologous recombination and is crucial to the maintenance of genome stability and biological diversity. The proteins RuvA, RuvB and RuvC play central roles in the late stage of recombination in prokaryotes. Recent atomic views of these proteins, including protein-protein and protein-junction DNA complexes, provide new insights into branch migration mechanisms: RuvA is likely to be responsible for base-pair rearrangements, whereas RuvB, classified as a member of the AAA(+) family, functions as a pump to pull DNA duplex arms without segmental unwinding. The mechanism of junction resolution by RuvC in the RuvABC resolvasome remains to be elucidated.

MeSH Terms
Bacterial Proteins/chemistry Base Sequence Binding Sites DNA Helicases/chemistry DNA, Bacterial/genetics DNA, Cruciform/chemistry DNA-Binding Proteins/chemistry Endodeoxyribonucleases/chemistry Escherichia coli/chemistry Escherichia coli Proteins/chemistry Models, Molecular Molecular Sequence Data Recombination, Genetic/genetics
Chemicals
Bacterial Proteins DNA, Bacterial DNA, Cruciform DNA-Binding Proteins Escherichia coli Proteins RuvB protein, Bacteria ruvC protein, E coli Endodeoxyribonucleases Holliday junction DNA helicase, E coli DNA Helicases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Yamada Kazuhiro
Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.
Ariyoshi Mariko
Morikawa Kosuke
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
2004-04-00
Pages
130-7
Language
English
Region
England
NLM ID
9107784
Subset
IM
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