ArticleJournal of the American Society for Mass Spectrometry2013
Escherichia coli single-stranded DNA-binding protein: nanoESI-MS studies of salt-modulated subunit exchange and DNA binding transactions.
Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- ATP is dispensable for E. coli DNA replication and eukaryotic helicase activity.Nature communications · 2026Article
- nCas9-based method for rolling-circle DNA substrate generation.Analytical biochemistry · 2025Article
- A bipartite interaction with the processivity clamp potentiates Pol IV-mediated TLS.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural characterisation of the complete cycle of sliding clamp loading in Escherichia coli.Nature communications · 2024Article
- A bipartite interaction with the processivity clamp potentiates Pol IV-mediated TLS.bioRxiv : the preprint server for biology · 2024Article
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- Single-molecule visualization of stalled replication-fork rescue by the Escherichia coli Rep helicase.Nucleic acids research · 2023Article
- Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Observing protein dynamics during DNA-lesion bypass by the replisome.Frontiers in molecular biosciences · 2022Review
- DnaB helicase dynamics in bacterial DNA replication resolved by single-molecule studies.Nucleic acids research · 2021Article
- A Primase-Induced Conformational Switch Controls the Stability of the Bacterial Replisome.Molecular cell · 2020Article
- Nuclease dead Cas9 is a programmable roadblock for DNA replication.Scientific reports · 2019Article
- Recycling of single-stranded DNA-binding protein by the bacterial replisome.Nucleic acids research · 2019Article
- The tale of SSB.Progress in biophysics and molecular biology · 2017Review
- Article
- The intrinsically disordered linker of E. coli SSB is critical for the release from single-stranded DNA.Protein science : a publication of the Protein Society · 2017Article
- Stability versus exchange: a paradox in DNA replication.Nucleic acids research · 2016Article
- Exchange between Escherichia coli polymerases II and III on a processivity clamp.Nucleic acids research · 2016Article
- Single-molecule studies of polymerase dynamics and stoichiometry at the bacteriophage T7 replication machinery.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Intramolecular binding mode of the C-terminus of Escherichia coli single-stranded DNA binding protein determined by nuclear magnetic resonance spectroscopy.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-stranded DNA-binding proteins (SSBs) are ubiquitous oligomeric proteins that bind with very high affinity to single-stranded DNA and have a variety of essential roles in DNA metabolism. Nanoelectrospray ionization mass spectrometry (nanoESI-MS) was used to monitor subunit exchange in full-length and truncated forms of the homotetrameric SSB from Escherichia coli. Subunit exchange in the native protein was found to occur slowly over a period of hours, but was significantly more rapid in a truncated variant of SSB from which the eight C-terminal residues were deleted. This effect is proposed to result from C-terminus mediated stabilization of the SSB tetramer, in which the C-termini interact with the DNA-binding cores of adjacent subunits. NanoESI-MS was also used to examine DNA binding to the SSB tetramer. Binding of single-stranded oligonucleotides [one molecule of (dT)(70), one molecule of (dT)(35), or two molecules of (dT)(35)] was found to prevent SSB subunit exchange. Transfer of SSB tetramers between discrete oligonucleotides was also observed and is consistent with predictions from solution-phase studies, suggesting that SSB-DNA complexes can be reliably analyzed by ESI mass spectrometry.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.