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Συνδεδεμένο Πλήρες Κείμενο

The bacterial MRE11-RAD50 and DNA2-WRN homologs process replication forks at distinct and separate loci on the chromosome.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: The bacterial MRE11-RAD50 and DNA2-WRN homologs process replication forks at distinct and separate loci on the chromosome.
Συγγραφείς: Spolek RL; Department of Biology, Portland State University, OR, USA., Christian PYH; Department of Biology, Portland State University, OR, USA., Courcelle CT; Department of Biology, Portland State University, OR, USA., Courcelle J; Department of Biology, Portland State University, OR, USA.
Πηγή: FEBS letters [FEBS Lett] 2026 Feb; Vol. 600 (4), pp. 451-466. Date of Electronic Publication: 2025 Oct 30.
Τύπος έκδοσης: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, N.I.H., Extramural
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3468 (Electronic) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
Imprint Name(s): Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
Ιατρικοί όροι (MeSH): Chromosomes, Bacterial*/metabolism , Escherichia coli*/metabolism , Escherichia coli Proteins*/metabolism , MRE11 Homologue Protein*/metabolism , DNA Damage Tolerance*, Acid Anhydride Hydrolases ; Werner Syndrome Helicase ; DNA-Binding Proteins ; DNA Helicases ; Deoxyribonucleases ; Exonucleases
Περίληψη: Human BRCA2 protects the DNA when replication forks stall, whereas MRE11-RAD50 and DNA2-WRN process or partially degrade these substrates. When mutated, these genes result in distinct genetic instabilities and cancers, arguing they have unique, not redundant, functions. Escherichia coli encodes functional homologs of MRE11-RAD50 (SbcC-SbcD), DNA2-WRN (RecJ-RecQ), and BRCA2 (RecF). Here, we use 2-dimensional gels, pulse-labelling, and replication-profiling analysis to show the bacterial homologs act at distinct substrates and loci on the chromosome. Whereas RecF and RecJ-RecQ protect and process DNA at arrested replication forks to facilitate repair, RecBCD and SbcC-SbcD protect and process DNA at sites where forks converge. Comparing the assays used in E. coli to human cells, we consider whether these cellular roles may be functionally conserved. Impact statement BRCA2, MRE11-RAD50, and WRN-DNA2 encode human proteins that process replication forks and result in distinct genetic instabilities and cancers when mutated. Here, we show their bacterial homologs act on unique replication fork substrates-those at DNA damage sites or as replication completes, and discuss their possible functional conservation in humans.
(© 2025 Federation of European Biochemical Societies.)
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Grant Information: R21 ES034880 United States ES NIEHS NIH HHS; R16 GM145543 United States GM NIGMS NIH HHS
Contributed Indexing: Keywords: DNA replication; DNA2‐WRN; MRE11–RAD50; RecJ–RecQ; SbcC–SbcD
Molecular Sequence: BioProject PRJNA1335257
Substance Nomenclature: EC 3.6.4.12 (DNA2 protein, human)
0 (Escherichia coli Proteins)
EC 3.1.- (MRE11 Homologue Protein)
0 (MRE11 protein, human)
EC 3.6.- (RAD50 protein, human)
0 (SbcC protein, E coli)
EC 3.1.- (sbcD protein, E coli)
EC 3.6.4.12 (WRN protein, human)
EC 3.6.- (Acid Anhydride Hydrolases)
EC 3.6.4.12 (Werner Syndrome Helicase)
0 (DNA-Binding Proteins)
EC 3.6.4.- (DNA Helicases)
EC 3.1.- (Deoxyribonucleases)
EC 3.1.- (Exonucleases)
Entry Date(s): Date Created: 20251031 Date Completed: 20260224 Latest Revision: 20260821
Update Code: 20260822
PubMed Central ID: PMC13050550
DOI: 10.1002/1873-3468.70211
PMID: 41168947
Βάση Δεδομένων: MEDLINE
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IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: The bacterial MRE11-RAD50 and DNA2-WRN homologs process replication forks at distinct and separate loci on the chromosome.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AU" term="%22Spolek+RL%22">Spolek RL</searchLink>; Department of Biology, Portland State University, OR, USA.<br /><searchLink fieldCode="AU" term="%22Christian+PYH%22">Christian PYH</searchLink>; Department of Biology, Portland State University, OR, USA.<br /><searchLink fieldCode="AU" term="%22Courcelle+CT%22">Courcelle CT</searchLink>; Department of Biology, Portland State University, OR, USA.<br /><searchLink fieldCode="AU" term="%22Courcelle+J%22">Courcelle J</searchLink>; Department of Biology, Portland State University, OR, USA.
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%220155157%22">FEBS letters</searchLink> [FEBS Lett] 2026 Feb; Vol. 600 (4), pp. 451-466. <i>Date of Electronic Publication: </i>2025 Oct 30.
– Name: TypePub
  Label: Publication Type
  Group: TypPub
  Data: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, N.I.H., Extramural
– Name: Language
  Label: Language
  Group: Lang
  Data: English
– Name: TitleSource
  Label: Journal Info
  Group: Src
  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22John+Wiley+%26+Sons+Ltd%22">John Wiley & Sons Ltd </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>0155157 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1873-3468 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200145793%22">00145793 </searchLink><i>NLM ISO Abbreviation: </i>FEBS Lett <i>Subsets: </i>MEDLINE
– Name: PublisherInfo
  Label: Imprint Name(s)
  Group: PubInfo
  Data: <i>Publication</i>: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.<br /><i>Original Publication</i>: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
– Name: SubjectMESH
  Label: MeSH Terms
  Group: Su
  Data: <searchLink fieldCode="MM" term="%22Chromosomes%2C+Bacterial%22">Chromosomes, Bacterial*</searchLink>/<searchLink fieldCode="MM" term="%22Chromosomes%2C+Bacterial+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Escherichia+coli%22">Escherichia coli*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Escherichia+coli+Proteins%22">Escherichia coli Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22MRE11+Homologue+Protein%22">MRE11 Homologue Protein*</searchLink>/<searchLink fieldCode="MM" term="%22MRE11+Homologue+Protein+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22DNA+Damage+Tolerance%22">DNA Damage Tolerance*</searchLink><br /><searchLink fieldCode="MH" term="%22Acid+Anhydride+Hydrolases%22">Acid Anhydride Hydrolases</searchLink> ; <searchLink fieldCode="MH" term="%22Werner+Syndrome+Helicase%22">Werner Syndrome Helicase</searchLink> ; <searchLink fieldCode="MH" term="%22DNA-Binding+Proteins%22">DNA-Binding Proteins</searchLink> ; <searchLink fieldCode="MH" term="%22DNA+Helicases%22">DNA Helicases</searchLink> ; <searchLink fieldCode="MH" term="%22Deoxyribonucleases%22">Deoxyribonucleases</searchLink> ; <searchLink fieldCode="MH" term="%22Exonucleases%22">Exonucleases</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Human BRCA2 protects the DNA when replication forks stall, whereas MRE11-RAD50 and DNA2-WRN process or partially degrade these substrates. When mutated, these genes result in distinct genetic instabilities and cancers, arguing they have unique, not redundant, functions. Escherichia coli encodes functional homologs of MRE11-RAD50 (SbcC-SbcD), DNA2-WRN (RecJ-RecQ), and BRCA2 (RecF). Here, we use 2-dimensional gels, pulse-labelling, and replication-profiling analysis to show the bacterial homologs act at distinct substrates and loci on the chromosome. Whereas RecF and RecJ-RecQ protect and process DNA at arrested replication forks to facilitate repair, RecBCD and SbcC-SbcD protect and process DNA at sites where forks converge. Comparing the assays used in E. coli to human cells, we consider whether these cellular roles may be functionally conserved. Impact statement BRCA2, MRE11-RAD50, and WRN-DNA2 encode human proteins that process replication forks and result in distinct genetic instabilities and cancers when mutated. Here, we show their bacterial homologs act on unique replication fork substrates-those at DNA damage sites or as replication completes, and discuss their possible functional conservation in humans.<br /> (© 2025 Federation of European Biochemical Societies.)
– Name: Ref
  Label: References
  Group: RefInfo
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– Name: GrantInfo
  Label: Grant Information
  Group: Grant
  Data: R21 ES034880 United States ES NIEHS NIH HHS; R16 GM145543 United States GM NIGMS NIH HHS
– Name: SubjectMinor
  Label: Contributed Indexing
  Group:
  Data: <i>Keywords: </i>DNA replication; DNA2‐WRN; MRE11–RAD50; RecJ–RecQ; SbcC–SbcD
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  Label: Molecular Sequence
  Group: ChemData
  Data: BioProject PRJNA1335257
– Name: NumberCAS
  Label: Substance Nomenclature
  Group: ID
  Data: EC 3.6.4.12 (DNA2 protein, human)<br />0 (Escherichia coli Proteins)<br />EC 3.1.- (MRE11 Homologue Protein)<br />0 (MRE11 protein, human)<br />EC 3.6.- (RAD50 protein, human)<br />0 (SbcC protein, E coli)<br />EC 3.1.- (sbcD protein, E coli)<br />EC 3.6.4.12 (WRN protein, human)<br />EC 3.6.- (Acid Anhydride Hydrolases)<br />EC 3.6.4.12 (Werner Syndrome Helicase)<br />0 (DNA-Binding Proteins)<br />EC 3.6.4.- (DNA Helicases)<br />EC 3.1.- (Deoxyribonucleases)<br />EC 3.1.- (Exonucleases)
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  Data: <i>Date Created: </i>20251031 <i>Date Completed: </i>20260224 <i>Latest Revision: </i>20260821
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  Data: 10.1002/1873-3468.70211
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        Value: 10.1002/1873-3468.70211
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 451
    Subjects:
      – SubjectFull: Acid Anhydride Hydrolases
        Type: general
      – SubjectFull: Werner Syndrome Helicase
        Type: general
      – SubjectFull: DNA-Binding Proteins
        Type: general
      – SubjectFull: DNA Helicases
        Type: general
      – SubjectFull: Deoxyribonucleases
        Type: general
      – SubjectFull: Exonucleases
        Type: general
      – SubjectFull: Chromosomes, Bacterial metabolism
        Type: general
      – SubjectFull: Escherichia coli metabolism
        Type: general
      – SubjectFull: Escherichia coli Proteins metabolism
        Type: general
      – SubjectFull: MRE11 Homologue Protein metabolism
        Type: general
      – SubjectFull: DNA Damage Tolerance
        Type: general
    Titles:
      – TitleFull: The bacterial MRE11-RAD50 and DNA2-WRN homologs process replication forks at distinct and separate loci on the chromosome.
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            – D: 01
              M: 02
              Text: 2026 Feb
              Type: published
              Y: 2026
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              Value: 1873-3468
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              Value: 600
            – Type: issue
              Value: 4
          Titles:
            – TitleFull: FEBS letters
              Type: main
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