We are analyzing https://link.springer.com/article/10.1007/s00412-010-0304-7.

Title:
Processing of joint molecule intermediates by structure-selective endonucleases during homologous recombination in eukaryotes | Chromosoma
Description:
Homologous recombination is required for maintaining genomic integrity by functioning in high-fidelity repair of DNA double-strand breaks and other complex lesions, replication fork support, and meiotic chromosome segregation. Joint DNA molecules are key intermediates in recombination and their differential processing determines whether the genetic outcome is a crossover or non-crossover event. The Holliday model of recombination highlights the resolution of four-way DNA joint molecules, termed Holliday junctions, and the bacterial Holliday junction resolvase RuvC set the paradigm for the mechanism of crossover formation. In eukaryotes, much effort has been invested in identifying the eukaryotic equivalent of bacterial RuvC, leading to the discovery of a number of DNA endonucleases, including Mus81–Mms4/EME1, Slx1–Slx4/BTBD12/MUS312, XPF–ERCC1, and Yen1/GEN1. These nucleases exert different selectivity for various DNA joint molecules, including Holliday junctions. Their mutant phenotypes and distinct species-specific characteristics expose a surprisingly complex system of joint molecule processing. In an attempt to reconcile the biochemical and genetic data, we propose that nicked junctions constitute important in vivo recombination intermediates whose processing determines the efficiency and outcome (crossover/non-crossover) of homologous recombination.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Science
Telecommunications

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We're unsure how the site profits.

Some websites aren't about earning revenue; they're built to connect communities or raise awareness. There are numerous motivations behind creating websites. This might be one of them. Link.springer.com might have a hidden revenue stream, but it's not something we can detect.

Keywords {🔍}

google, scholar, pubmed, cas, article, dna, yeast, repair, mus, recombination, meiotic, holliday, endonuclease, slx, cleavage, rad, replication, hjs, cell, junction, junctions, fig, cerevisiae, budding, formation, protein, substrate, heyer, cells, role, mutants, analysis, nicked, biol, model, mol, substrates, intermediates, double, ruvc, activity, genetics, human, joint, endonucleases, complex, genetic, resolution, saccharomyces, brill,

Topics {✒️}

381-amino-acid c-terminal truncation helix–hairpin–helix protein involved microhomology-mediated end-joining double-strand break-induced recombination sce-i-induced dsb formation double-strand-break repair model article download pdf purified mus81–mms4/eme1 complexes conserved c-terminal region full-length component strand hhmi-imbs training grant conserved coiled–coil domain xpf–ercc1–slx4 complex functions full-length human gen1 single-strand annealing mode full-length proteins complicate giy–yig nuclease superfamily rad2 family endo-exonuclease double-strand break repair full size image single-stranded gaps created double-strand break recombination purified full-length dmgen dna double-strand breaks human mus81/eme1 endonuclease dna structure-selective endonucleases structure-selective dna endonucleases synthesis-dependent strand annealing human mus81–eme1 complex break-induced dna replication recombination-mediated dna repair methylation-induced dna damage identical n-terminal truncations mus81–mms4/eme1 endonucleases including mus81–mms4/eme1 mus81–mms4/eme1 endonuclease general recombination-mediated repair dna structure-specific endonucleases catalytically active mus81–mms4 dna damage-induced phosphorylation lagging-strand replication defects mus81–mms4/eme1 complex mec1-dependent rtt107 phosphorylation catalytic structure-selective endonuclease classical michaelis–menten analysis human mus81–eme1 acting conserved muts-based pathway homologous endonuclease rad1–rad10 mec1/tel1-dependent phosphorylation rad2/xpg endonuclease family

Questions {❓}

Gaskell LJ, Osman F, Gilbert RJ, Whitby MC (2007) Mus81 cleavage of Holliday junctions: a failsafe for processing meiotic recombination intermediates?
Heyer WD, Ehmsen KT, Solinger JA (2003) Holliday junctions in the eukaryotic nucleus: resolution in sight?
How can the processing of nicked junctions lead to COs?
If HJs are the dominating recombination structure, then why is the phenotype of the only eukaryotic enzyme, Yen1, with characteristics of the RuvC resolvase so inconspicuous?
Maybe the paradigm that HJs, single or double, comprise four uninterrupted strands is too narrow?
The complexity of DNA structure-selective endonucleases involved in DNA repair, replication, and recombination is surprising, suggesting that the various enzymes address different junction types or similar junctions occurring in different compartments (nucleus, nucleolus, mitochondria?
West SC (1995) Holliday junctions cleaved by Rad1?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Processing of joint molecule intermediates by structure-selective endonucleases during homologous recombination in eukaryotes
         description:Homologous recombination is required for maintaining genomic integrity by functioning in high-fidelity repair of DNA double-strand breaks and other complex lesions, replication fork support, and meiotic chromosome segregation. Joint DNA molecules are key intermediates in recombination and their differential processing determines whether the genetic outcome is a crossover or non-crossover event. The Holliday model of recombination highlights the resolution of four-way DNA joint molecules, termed Holliday junctions, and the bacterial Holliday junction resolvase RuvC set the paradigm for the mechanism of crossover formation. In eukaryotes, much effort has been invested in identifying the eukaryotic equivalent of bacterial RuvC, leading to the discovery of a number of DNA endonucleases, including Mus81–Mms4/EME1, Slx1–Slx4/BTBD12/MUS312, XPF–ERCC1, and Yen1/GEN1. These nucleases exert different selectivity for various DNA joint molecules, including Holliday junctions. Their mutant phenotypes and distinct species-specific characteristics expose a surprisingly complex system of joint molecule processing. In an attempt to reconcile the biochemical and genetic data, we propose that nicked junctions constitute important in vivo recombination intermediates whose processing determines the efficiency and outcome (crossover/non-crossover) of homologous recombination.
         datePublished:2011-01-11T00:00:00Z
         dateModified:2011-01-11T00:00:00Z
         pageStart:109
         pageEnd:127
         license:https://creativecommons.org/licenses/by-nc/2.0
         sameAs:https://doi.org/10.1007/s00412-010-0304-7
         keywords:
            Homologous Recombination
            Nucleotide Excision Repair
            Fission Yeast
            Replication Fork
            Synthetic Lethality
            Cell Biology
            Developmental Biology
            Biochemistry
            general
            Human Genetics
            Animal Genetics and Genomics
            Eukaryotic Microbiology
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig1_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig2_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig3_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig4_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig5_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig6_HTML.gif
         isPartOf:
            name:Chromosoma
            issn:
               1432-0886
               0009-5915
            volumeNumber:120
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer-Verlag
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Erin K. Schwartz
               affiliation:
                     name:University of California—Davis
                     address:
                        name:Department of Microbiology, University of California—Davis, Davis, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Wolf-Dietrich Heyer
               affiliation:
                     name:University of California—Davis
                     address:
                        name:Department of Microbiology, University of California—Davis, Davis, USA
                        type:PostalAddress
                     type:Organization
                     name:University of California—Davis
                     address:
                        name:Department of Molecular and Cellular Biology, University of California—Davis, Davis, USA
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:1
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Processing of joint molecule intermediates by structure-selective endonucleases during homologous recombination in eukaryotes
      description:Homologous recombination is required for maintaining genomic integrity by functioning in high-fidelity repair of DNA double-strand breaks and other complex lesions, replication fork support, and meiotic chromosome segregation. Joint DNA molecules are key intermediates in recombination and their differential processing determines whether the genetic outcome is a crossover or non-crossover event. The Holliday model of recombination highlights the resolution of four-way DNA joint molecules, termed Holliday junctions, and the bacterial Holliday junction resolvase RuvC set the paradigm for the mechanism of crossover formation. In eukaryotes, much effort has been invested in identifying the eukaryotic equivalent of bacterial RuvC, leading to the discovery of a number of DNA endonucleases, including Mus81–Mms4/EME1, Slx1–Slx4/BTBD12/MUS312, XPF–ERCC1, and Yen1/GEN1. These nucleases exert different selectivity for various DNA joint molecules, including Holliday junctions. Their mutant phenotypes and distinct species-specific characteristics expose a surprisingly complex system of joint molecule processing. In an attempt to reconcile the biochemical and genetic data, we propose that nicked junctions constitute important in vivo recombination intermediates whose processing determines the efficiency and outcome (crossover/non-crossover) of homologous recombination.
      datePublished:2011-01-11T00:00:00Z
      dateModified:2011-01-11T00:00:00Z
      pageStart:109
      pageEnd:127
      license:https://creativecommons.org/licenses/by-nc/2.0
      sameAs:https://doi.org/10.1007/s00412-010-0304-7
      keywords:
         Homologous Recombination
         Nucleotide Excision Repair
         Fission Yeast
         Replication Fork
         Synthetic Lethality
         Cell Biology
         Developmental Biology
         Biochemistry
         general
         Human Genetics
         Animal Genetics and Genomics
         Eukaryotic Microbiology
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig1_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig2_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig3_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig4_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig5_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00412-010-0304-7/MediaObjects/412_2010_304_Fig6_HTML.gif
      isPartOf:
         name:Chromosoma
         issn:
            1432-0886
            0009-5915
         volumeNumber:120
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Springer-Verlag
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Erin K. Schwartz
            affiliation:
                  name:University of California—Davis
                  address:
                     name:Department of Microbiology, University of California—Davis, Davis, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Wolf-Dietrich Heyer
            affiliation:
                  name:University of California—Davis
                  address:
                     name:Department of Microbiology, University of California—Davis, Davis, USA
                     type:PostalAddress
                  type:Organization
                  name:University of California—Davis
                  address:
                     name:Department of Molecular and Cellular Biology, University of California—Davis, Davis, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:1
["Periodical","PublicationVolume"]:
      name:Chromosoma
      issn:
         1432-0886
         0009-5915
      volumeNumber:120
Organization:
      name:Springer-Verlag
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of California—Davis
      address:
         name:Department of Microbiology, University of California—Davis, Davis, USA
         type:PostalAddress
      name:University of California—Davis
      address:
         name:Department of Microbiology, University of California—Davis, Davis, USA
         type:PostalAddress
      name:University of California—Davis
      address:
         name:Department of Molecular and Cellular Biology, University of California—Davis, Davis, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Erin K. Schwartz
      affiliation:
            name:University of California—Davis
            address:
               name:Department of Microbiology, University of California—Davis, Davis, USA
               type:PostalAddress
            type:Organization
      name:Wolf-Dietrich Heyer
      affiliation:
            name:University of California—Davis
            address:
               name:Department of Microbiology, University of California—Davis, Davis, USA
               type:PostalAddress
            type:Organization
            name:University of California—Davis
            address:
               name:Department of Molecular and Cellular Biology, University of California—Davis, Davis, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Microbiology, University of California—Davis, Davis, USA
      name:Department of Microbiology, University of California—Davis, Davis, USA
      name:Department of Molecular and Cellular Biology, University of California—Davis, Davis, USA

External Links {🔗}(468)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

5.5s.

LINK . SPRINGER . COM {}