scholarly journals Structural Study on Homologous Recombination: Recognition Mechanism of Holliday Junction by E. coli RuvA.

2002 ◽  
Vol 42 (1) ◽  
pp. 4-8
Author(s):  
Mariko ARIYOSHI
Keyword(s):  
Homologous Recombination ◽  
Structural Study ◽  
Holliday Junction ◽  
Recognition Mechanism ◽  
E Coli

scholarly journals Single bacterial resolvases first exploit, then constrain intrinsic dynamics of the Holliday junction to direct recombination

2021 ◽  
Author(s):  
Sujay Ray ◽  
Nibedita Pal ◽  
Nils G Walter
Keyword(s):  
Cluster Analysis ◽  
Homologous Recombination ◽  
Single Molecule ◽  
Holliday Junction ◽  
Energetic Cost ◽  
Genomic Integrity ◽  
Dna Molecules ◽  
Single Molecule Fluorescence ◽  
And Cluster Analysis ◽  
Fluorescence Observation

Abstract Homologous recombination forms and resolves an entangled DNA Holliday Junction (HJ) crucial for achieving genetic reshuffling and genome repair. To maintain genomic integrity, specialized resolvase enzymes cleave the entangled DNA into two discrete DNA molecules. However, it is unclear how two similar stacking isomers are distinguished, and how a cognate sequence is found and recognized to achieve accurate recombination. We here use single-molecule fluorescence observation and cluster analysis to examine how prototypic bacterial resolvase RuvC singles out two of the four HJ strands and achieves sequence-specific cleavage. We find that RuvC first exploits, then constrains the dynamics of intrinsic HJ isomer exchange at a sampled branch position to direct cleavage toward the catalytically competent HJ conformation and sequence, thus controlling recombination output at minimal energetic cost. Our model of rapid DNA scanning followed by ‘snap-locking’ of a cognate sequence is strikingly consistent with the conformational proofreading of other DNA-modifying enzymes.

scholarly journals A defect in homologous recombination leads to increased translesion synthesisin E. coli

2016 ◽  
Vol 44 (16) ◽  
pp. 7691-7699 ◽  
Author(s):  
Karel Naiman ◽  
Vincent Pagès ◽  
Robert P. Fuchs
Keyword(s):  
Homologous Recombination ◽  
E Coli

Crystallization of E. coli RuvA gives insights into the symmetry of a Holliday junction/protein complex

1997 ◽  
Vol 53 (1) ◽  
pp. 122-124 ◽  
Author(s):  
S. E. Sedelnikova ◽  
J. B. Rafferty ◽  
D. Hargreaves ◽  
A. A. Mahdi ◽  
R. G. Lloyd ◽  
...  
Keyword(s):  
Protein Complex ◽  
Holliday Junction ◽  
E Coli ◽  
Junction Protein

An efficient method for precise gene substitution in the AcMNPV genome by homologous recombination in E. coli

2003 ◽  
Vol 113 (2) ◽  
pp. 95-101 ◽  
Author(s):  
Wuwei Wu ◽  
Jinwen Wang ◽  
Riqiang Deng ◽  
Xunzhang Wang ◽  
XiongLei He ◽  
...  
Keyword(s):  
Homologous Recombination ◽  
Efficient Method ◽  
Gene Substitution ◽  
E Coli

scholarly journals Use of Recombination-Mediated Genetic Engineering for Construction of Rescue Human Cytomegalovirus Bacterial Artificial Chromosome Clones

2012 ◽  
Vol 2012 ◽  
pp. 1-10 ◽  
Author(s):  
Kalpana Dulal ◽  
Benjamin Silver ◽  
Hua Zhu
Keyword(s):  
Bacterial Artificial Chromosome ◽  
Homologous Recombination ◽  
Human Cytomegalovirus ◽  
Artificial Chromosome ◽  
Bac Clone ◽  
Dna Viruses ◽  
E Coli ◽  
Recombination System ◽  
Capture Method

Bacterial artificial chromosome (BAC) technology has contributed immensely to manipulation of larger genomes in many organisms including large DNA viruses like human cytomegalovirus (HCMV). The HCMV BAC clone propagated and maintained insideE. coliallows for accurate recombinant virus generation. Using this system, we have generated a panel of HCMV deletion mutants and their rescue clones. In this paper, we describe the construction of HCMV BAC mutants using a homologous recombination system. A gene capture method, or gap repair cloning, to seize large fragments of DNA from the virus BAC in order to generate rescue viruses, is described in detail. Construction of rescue clones using gap repair cloning is highly efficient and provides a novel use of the homologous recombination-based method inE. colifor molecular cloning, known colloquially as recombineering, when rescuing large BAC deletions. This method of excising large fragments of DNA provides important prospects forin vitrohomologous recombination for genetic cloning.

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

Cell ◽  
1994 ◽  
Vol 78 (6) ◽  
pp. 1063-1072 ◽  
Author(s):  
Mariko Ariyoshi ◽  
Dmitry G. Vassylyev ◽  
Hiroshi Iwasaki ◽  
Haruki Nakamura ◽  
Hideo Shinagawa ◽  
...  
Keyword(s):  
Atomic Structure ◽  
Holliday Junction ◽  
E Coli

scholarly journals DNA replication triggered by double-stranded breaks in E. coli: Dependence on homologous recombination functions

Cell ◽  
1994 ◽  
Vol 78 (6) ◽  
pp. 1051-1061 ◽  
Author(s):  
Tsuneaki Asai ◽  
David B. Bates ◽  
Tokio Kogoma
Keyword(s):  
Dna Replication ◽  
Homologous Recombination ◽  
E Coli

scholarly journals Assembly of Radically Recoded E. coli Genome Segments

2016 ◽  
Author(s):  
Julie E. Norville ◽  
Cameron L. Gardner ◽  
Eduardo Aponte ◽  
Conor K. Camplisson ◽  
Alexandra Gonzales ◽  
...  
Keyword(s):  
Homologous Recombination ◽  
Genome Engineering ◽  
Next Generation ◽  
Selective Marker ◽  
E Coli ◽  
Cassette Exchange ◽  
Large Potential ◽  
Attachment Sites

AbstractThe large potential of radically recoded organisms (RROs) in medicine and industry depends on improved technologies for efficient assembly and testing of recoded genomes for biosafety and functionality. Here we describe a next generation platform for conjugative assembly genome engineering, termed CAGE 2.0, that enables the scarless integration of large synthetically recoded E. coli segments at isogenic and adjacent genomic loci. A stable tdk dual selective marker is employed to facilitate cyclical assembly and removal of attachment sites used for targeted segment delivery by sitespecific recombination. Bypassing the need for vector transformation harnesses the multi Mb capacity of CAGE, while minimizing artifacts associated with RecA-mediated homologous recombination. Our method expands the genome engineering toolkit for radical modification across many organisms and recombinase-mediated cassette exchange (RMCE).

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