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    tus DNA replication terminus site-binding protein [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945135, updated on 17-Dec-2024

    Summary

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    Official Symbol
    tus
    Official Full Name
    DNA replication terminus site-binding protein
    Primary source
    ECOCYC:EG11038
    Locus tag
    b1610
    See related
    ASAP:ABE-0005378
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK1605; tau
    Summary
    Site-specific DNA binding protein Tus arrests the DnaB helicase at six chromosomal Ter sites (A-F), blocking replication forks. [More information is available at EcoGene: EG11038]. Tus, also known as ter-binding protein (TBP), binds to ter sites, blocking the progress of DNA replication in a polar fashion, thus terminating replication . [More information is available at EcoCyc: EG11038].
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    Genomic context

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    Sequence:
    NC_000913.3 (1684259..1685188)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional regulator RstA Neighboring gene sensory histidine kinase RstB Neighboring gene fumarase C Neighboring gene fumarase A Neighboring gene mannose-6-phosphate isomerase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The contrahelicase activities of the replication terminator proteins of Escherichia coli and Bacillus subtilis are helicase-specific and impede both helicase translocation and authentic DNA unwinding. Sahoo T, et al. J Biol Chem, 1995 Dec 8. PMID 7493939
    2. Sequence-specific interactions in the Tus-Ter complex and the effect of base pair substitutions on arrest of DNA replication in Escherichia coli. Coskun-Ari FF, et al. J Biol Chem, 1997 Oct 17. PMID 9334221
    3. Inactivation of the replication-termination system affects the replication mode and causes unstable maintenance of plasmid R1. Krabbe M, et al. Mol Microbiol, 1997 May. PMID 9194700
    4. A tale of two terminators: crystal structures sharpen the debate on DNA replication fork arrest mechanisms. Wake R, et al. Structure, 1997 Jan 15. PMID 9016713
    5. The progression of replication forks at natural replication barriers in live bacteria. Moolman MC, et al. Nucleic Acids Res, 2016 Jul 27. PMID 27166373, Free PMC Article

    See all (65) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. We demonstrate that the replisome remains stably bound after encountering a Tus-ter complex from the non-permissive direction. Furthermore, the replisome is only transiently blocked, and continues replication beyond the barrier. Additionally, we demonstrate that these barriers affect sister chromosome segregation by visualizing specific chromosomal loci in the presence and absence of the Tus protein.
      Title: The progression of replication forks at natural replication barriers in live bacteria.
    2. The study presents a model for replication fork arrest by the Escherichia coli Tus-Ter complex.
      Title: Two mechanisms coordinate replication termination by the Escherichia coli Tus-Ter complex.
    3. N-terminus verified by Edman degradation on mature peptide
      Title: Purification of a DNA replication terminus (ter) site-binding protein in Escherichia coli and identification of the structural gene.
    4. Data suggest that increased negative supercoiling enhances DnaB unwinding activity, thereby reducing the duration of the Tus-DnaB interaction and leading to decreased Tus activity.
      Title: Tus-mediated arrest of DNA replication in Escherichia coli is modulated by DNA supercoiling.
    5. As the replication fork helicase unwinds one side of the DNA sequence Ter, a conserved cytosine flips out of the duplex and binds to Tus, thereby creating a locked complex that blocks the advancing helicase.
      Title: Replication termination: mechanism of polar arrest revealed.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables sequence-specific DNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in DNA replication IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within DNA replication termination IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in DNA replication termination IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within replication fork arrest involved in DNA replication termination IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    DNA replication terminus site-binding protein

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      1684259..1685188
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416127.1 DNA replication terminus site-binding protein [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416127.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A776LNV3, A0A8S7EIC5
      Conserved Domains (1) summary
      PRK02951
      Location:1 → 309
      PRK02951; DNA replication terminus site-binding protein; Provisional
    Nucleotide Protein
    Heading Accession and Version

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