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  1. Article ; Online: The intrinsically disordered linker in the single-stranded DNA-binding protein influences DNA replication restart and recombination pathways in

    Sandler, Steven J / Bonde, Nina J / Wood, Elizabeth A / Cox, Michael M / Keck, James L

    Journal of bacteriology

    2024  Volume 206, Issue 4, Page(s) e0033023

    Abstract: Tetrameric single-stranded (ss) DNA-binding proteins (SSBs) stabilize ssDNA intermediates formed during genome maintenance reactions ... ...

    Abstract Tetrameric single-stranded (ss) DNA-binding proteins (SSBs) stabilize ssDNA intermediates formed during genome maintenance reactions in
    MeSH term(s) Escherichia coli/genetics ; Escherichia coli K12/genetics ; Escherichia coli Proteins/metabolism ; DNA-Binding Proteins/metabolism ; DNA Replication ; DNA/metabolism ; DNA, Single-Stranded/metabolism ; Recombination, Genetic
    Chemical Substances Escherichia coli Proteins ; DNA-Binding Proteins ; DNA (9007-49-2) ; DNA, Single-Stranded ; PriC protein, E coli (146312-41-6) ; PriB protein, E coli
    Language English
    Publishing date 2024-03-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/jb.00330-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.50: Show issues Location:
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  2. Article ; Online: Interaction with the carboxy-terminal tip of SSB is critical for RecG function in E. coli.

    Bonde, Nina J / Henry, Camille / Wood, Elizabeth A / Cox, Michael M / Keck, James L

    Nucleic acids research

    2023  Volume 51, Issue 8, Page(s) 3735–3753

    Abstract: In Escherichia coli, the single-stranded DNA-binding protein (SSB) acts as a genome maintenance organizational hub by interacting with multiple DNA metabolism proteins. Many SSB-interacting proteins (SIPs) form complexes with SSB by docking onto its ... ...

    Abstract In Escherichia coli, the single-stranded DNA-binding protein (SSB) acts as a genome maintenance organizational hub by interacting with multiple DNA metabolism proteins. Many SSB-interacting proteins (SIPs) form complexes with SSB by docking onto its carboxy-terminal tip (SSB-Ct). An alternative interaction mode in which SIPs bind to PxxP motifs within an intrinsically-disordered linker (IDL) in SSB has been proposed for the RecG DNA helicase and other SIPs. Here, RecG binding to SSB and SSB peptides was measured in vitro and the RecG/SSB interface was identified. The results show that RecG binds directly and specifically to the SSB-Ct, and not the IDL, through an evolutionarily conserved binding site in the RecG helicase domain. Mutations that block RecG binding to SSB sensitize E. coli to DNA damaging agents and induce the SOS DNA-damage response, indicating formation of the RecG/SSB complex is important in vivo. The broader role of the SSB IDL is also investigated. E. coli ssb mutant strains encoding SSB IDL deletion variants lacking all PxxP motifs retain wildtype growth and DNA repair properties, demonstrating that the SSB PxxP motifs are not major contributors to SSB cellular functions.
    MeSH term(s) Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; DNA Helicases/genetics ; DNA Repair ; Binding Sites ; DNA, Single-Stranded/genetics ; DNA, Single-Stranded/metabolism ; Protein Binding ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism
    Chemical Substances Escherichia coli Proteins ; DNA Helicases (EC 3.6.4.-) ; DNA, Single-Stranded ; RecG protein, E coli (145137-68-4) ; SSB protein, E coli ; DNA-Binding Proteins
    Language English
    Publishing date 2023-03-04
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkad162
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1067: Show issues Location:
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  3. Article ; Online: RadD is a RecA-dependent accessory protein that accelerates DNA strand exchange.

    Bonde, Nina J / Romero, Zachary J / Chitteni-Pattu, Sindhu / Cox, Michael M

    Nucleic acids research

    2022  Volume 50, Issue 4, Page(s) 2201–2210

    Abstract: In rapidly growing cells, with recombinational DNA repair required often and a new replication fork passing every 20 min, the pace of RecA-mediated DNA strand exchange is potentially much too slow for bacterial DNA metabolism. The enigmatic RadD protein, ...

    Abstract In rapidly growing cells, with recombinational DNA repair required often and a new replication fork passing every 20 min, the pace of RecA-mediated DNA strand exchange is potentially much too slow for bacterial DNA metabolism. The enigmatic RadD protein, a putative SF2 family helicase, exhibits no independent helicase activity on branched DNAs. Instead, RadD greatly accelerates RecA-mediated DNA strand exchange, functioning only when RecA protein is present. The RadD reaction requires the RadD ATPase activity, does not require an interaction with SSB, and may disassemble RecA filaments as it functions. We present RadD as a new class of enzyme, an accessory protein that accelerates DNA strand exchange, possibly with a helicase-like action, in a reaction that is entirely RecA-dependent. RadD is thus a DNA strand exchange (recombination) synergist whose primary function is to coordinate closely with and accelerate the DNA strand exchange reactions promoted by the RecA recombinase. Multiple observations indicate a uniquely close coordination of RadD with RecA function.
    MeSH term(s) Adenosine Triphosphatases/genetics ; DNA/genetics ; DNA/metabolism ; DNA, Bacterial/genetics ; DNA, Bacterial/metabolism ; DNA, Single-Stranded/genetics ; DNA, Single-Stranded/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Rec A Recombinases/genetics ; Rec A Recombinases/metabolism
    Chemical Substances DNA, Bacterial ; DNA, Single-Stranded ; DNA (9007-49-2) ; Rec A Recombinases (EC 2.7.7.-) ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2022-02-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkac041
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
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  4. Article ; Online: Identification of

    Bonde, Nina J / Wood, Elizabeth A / Myers, Kevin S / Place, Michael / Keck, James L / Cox, Michael M

    Journal of bacteriology

    2023  Volume 205, Issue 12, Page(s) e0018423

    Abstract: Importance: DNA damage and subsequent DNA repair processes are mutagenic in nature and an important driver of evolution in prokaryotes, including antibiotic resistance development. Genetic screening approaches, such as transposon sequencing (Tn-seq), ... ...

    Abstract Importance: DNA damage and subsequent DNA repair processes are mutagenic in nature and an important driver of evolution in prokaryotes, including antibiotic resistance development. Genetic screening approaches, such as transposon sequencing (Tn-seq), have provided important new insights into gene function and genetic relationships. Here, we employed Tn-seq to gain insight into the function of the
    MeSH term(s) Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; DNA Helicases/genetics ; DNA Repair ; DNA Damage ; Bacterial Proteins/genetics
    Chemical Substances Escherichia coli Proteins ; DNA Helicases (EC 3.6.4.-) ; Bacterial Proteins
    Language English
    Publishing date 2023-11-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/jb.00184-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.50: Show issues Location:
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  5. Article ; Online: RecF protein targeting to post-replication (daughter strand) gaps II: RecF interaction with replisomes.

    Henry, Camille / Kaur, Gurleen / Cherry, Megan E / Henrikus, Sarah S / Bonde, Nina J / Sharma, Nischal / Beyer, Hope A / Wood, Elizabeth A / Chitteni-Pattu, Sindhu / van Oijen, Antoine M / Robinson, Andrew / Cox, Michael M

    Nucleic acids research

    2023  Volume 51, Issue 11, Page(s) 5714–5742

    Abstract: The bacterial RecF, RecO, and RecR proteins are an epistasis group involved in loading RecA protein into post-replication gaps. However, the targeting mechanism that brings these proteins to appropriate gaps is unclear. Here, we propose that targeting ... ...

    Abstract The bacterial RecF, RecO, and RecR proteins are an epistasis group involved in loading RecA protein into post-replication gaps. However, the targeting mechanism that brings these proteins to appropriate gaps is unclear. Here, we propose that targeting may involve a direct interaction between RecF and DnaN. In vivo, RecF is commonly found at the replication fork. Over-expression of RecF, but not RecO or a RecF ATPase mutant, is extremely toxic to cells. We provide evidence that the molecular basis of the toxicity lies in replisome destabilization. RecF over-expression leads to loss of genomic replisomes, increased recombination associated with post-replication gaps, increased plasmid loss, and SOS induction. Using three different methods, we document direct interactions of RecF with the DnaN β-clamp and DnaG primase that may underlie the replisome effects. In a single-molecule rolling-circle replication system in vitro, physiological levels of RecF protein trigger post-replication gap formation. We suggest that the RecF interactions, particularly with DnaN, reflect a functional link between post-replication gap creation and gap processing by RecA. RecF's varied interactions may begin to explain how the RecFOR system is targeted to rare lesion-containing post-replication gaps, avoiding the potentially deleterious RecA loading onto thousands of other gaps created during replication.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; DNA Repair ; DNA Replication ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism
    Chemical Substances Bacterial Proteins ; DNA-Binding Proteins ; Escherichia coli Proteins ; recF protein, E coli
    Language English
    Publishing date 2023-05-02
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkad310
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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