SSB as an organizer/mobilizer of genome maintenance complexes
When duplex DNA is altered in almost any way (replicated, recombined, or repaired), single
strands of DNA are usually intermediates, and single-stranded DNA binding (SSB) proteins …
strands of DNA are usually intermediates, and single-stranded DNA binding (SSB) proteins …
Regulation of bacterial RecA protein function
MM Cox - Critical reviews in biochemistry and molecular biology, 2007 - Taylor & Francis
The RecA protein is a recombinase functioning in recombinational DNA repair in bacteria.
RecA is regulated at many levels. The expression of the recA gene is regulated within the …
RecA is regulated at many levels. The expression of the recA gene is regulated within the …
Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members
We report an in-depth computational study of the protein sequences and structures of the
superfamily of archaeo-eukaryotic primases (AEPs). This analysis greatly expands the range …
superfamily of archaeo-eukaryotic primases (AEPs). This analysis greatly expands the range …
Interaction with the carboxy-terminal tip of SSB is critical for RecG function in E. coli
NJ Bonde, C Henry, EA Wood, MM Cox… - Nucleic Acids …, 2023 - academic.oup.com
In Escherichia coli, the single-stranded DNA-binding protein (SSB) acts as a genome
maintenance organizational hub by interacting with multiple DNA metabolism proteins …
maintenance organizational hub by interacting with multiple DNA metabolism proteins …
PriA helicase and SSB interact physically and functionally
CJ Cadman, P McGlynn - Nucleic acids research, 2004 - academic.oup.com
PriA helicase is the major DNA replication restart initiator in Escherichia coli and acts to
reload the replicative helicase DnaB back onto the chromosome at repaired replication forks …
reload the replicative helicase DnaB back onto the chromosome at repaired replication forks …
The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks
A Costes, F Lecointe, S McGovern… - PLoS …, 2010 - journals.plos.org
We have investigated in vivo the role of the carboxy-terminal domain of the Bacillus subtilis
Single-Stranded DNA Binding protein (SSBCter) as a recruitment platform at active …
Single-Stranded DNA Binding protein (SSBCter) as a recruitment platform at active …
A central role for SSB in Escherichia coli RecQ DNA helicase function
RecQ DNA helicases are critical components of DNA replication, recombination, and repair
machinery in all eukaryotes and bacteria. Eukaryotic RecQ helicases are known to associate …
machinery in all eukaryotes and bacteria. Eukaryotic RecQ helicases are known to associate …
Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine
Single-stranded DNA-binding proteins (SSBs) are required for repair, recombination and
replication in all organisms. Eukaryotic SSBs are regulated by phosphorylation on serine …
replication in all organisms. Eukaryotic SSBs are regulated by phosphorylation on serine …
The C‐terminal domain of full‐length E. coli SSB is disordered even when bound to DNA
The crystal structure of full‐length homotetrameric single‐stranded DNA (ssDNA)‐binding
protein from Escherichia coli (SSB) has been determined to 3.3 Å resolution and reveals that …
protein from Escherichia coli (SSB) has been determined to 3.3 Å resolution and reveals that …
The mechanism of action of the SSB interactome reveals it is the first OB‐fold family of genome guardians in prokaryotes
PR Bianco - Protein science, 2021 - Wiley Online Library
The single‐stranded DNA binding protein (SSB) is essential to all aspects of DNA
metabolism in bacteria. This protein performs two distinct, but closely intertwined and …
metabolism in bacteria. This protein performs two distinct, but closely intertwined and …