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    priA primosomal protein N' [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948426, updated on 3-Dec-2024

    Summary

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    Official Symbol
    priA
    Official Full Name
    primosomal protein N'
    Primary source
    ECOCYC:EG10763
    Locus tag
    b3935
    See related
    ASAP:ABE-0012860
    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
    ECK3927; srgA
    Summary
    The role of PriA in the cell appears to be the restart of stalled replication forks. [More information is available at EcoCyc: EG10763].
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    Genomic context

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    Sequence:
    NC_000913.3 (4124612..4126810, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene cell division protein FtsN Neighboring gene DNA-binding transcriptional repressor CytR Neighboring gene 50S ribosomal subunit protein L31 Neighboring gene putative lipid-binding hydrolase YiiX

    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. Escherichia coli factor Y sites of plasmid pBR322 can function as origins of DNA replication. Zipursky SL, et al. Proc Natl Acad Sci U S A, 1981 Oct. PMID 6273849, Free PMC Article
    2. Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli. Sasaki K, et al. Biochim Biophys Acta, 2006 Jan. PMID 16226927
    3. Multistep sequential mechanism of Escherichia coli helicase PriA protein-ssDNA interactions. Kinetics and energetics of the active ssDNA-searching site of the enzyme. Galletto R, et al. Biochemistry, 2004 Aug 31. PMID 15323559
    4. A critical role of the 3' terminus of nascent DNA chains in recognition of stalled replication forks. Mizukoshi T, et al. J Biol Chem, 2003 Oct 24. PMID 12917421
    5. Connecting replication and recombination. Lovett ST. Mol Cell, 2003 Mar. PMID 12667440

    See all (110) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Identification of genetic interactions with priB links the PriA/PriB DNA replication restart pathway to double-strand DNA break repair in Escherichia coli.
      Title: Identification of genetic interactions with priB links the PriA/PriB DNA replication restart pathway to double-strand DNA break repair in Escherichia coli.
    2. Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
      Title: Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
    3. Mutational Analysis of Residues in PriA and PriC Affecting Their Ability To Interact with SSB in Escherichia coli K-12.
      Title: Mutational Analysis of Residues in PriA and PriC Affecting Their Ability To Interact with SSB in Escherichia coli K-12.
    4. DNA Helicase-SSB Interactions Critical to the Regression and Restart of Stalled DNA Replication forks in Escherichia coli.
      Title: DNA Helicase-SSB Interactions Critical to the Regression and Restart of Stalled DNA Replication forks in Escherichia coli.
    5. observations lead to a model in which coordinated parental-, leading-, and lagging-strand DNA binding provide PriA with the structural specificity needed to act on abandoned DNA replication forks.
      Title: Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.
    6. Both the N-terminal and the C-terminal fragments of PriA are required for activity, and the N-terminal fragment can be optimized to yield wild-type activity.
      Title: A priA Mutant Expressed in Two Pieces Has Almost Full Activity in Escherichia coli K-12.
    7. We speculate that replication pausing and fork-slow-down shortly after initiation may represent a novel checkpoint that ensures the presence of sufficient nucleotide supply prior to commitment to duplication of the entire genome.
      Title: Fork restart protein, PriA, binds around oriC after depletion of nucleotide precursors: Replication fork arrest near the replication origin.
    8. Data show that single-stranded DNA binding proteins (SSB)-interacting proteins RecO, RecG, PriA, and accessory helicase Rep do not correlate with replication at relication forks.
      Title: Are the SSB-Interacting Proteins RecO, RecG, PriA and the DnaB-Interacting Protein Rep Bound to Progressing Replication Forks in Escherichia coli?
    9. Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.
      Title: Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.
    10. A small number of interacting nucleotides indicates that the DNA-binding subsites of the PriA helicase, i.e., the strong subsite on the helicase domain and the weak subsite on the N-terminal domain, are spatially separated in the intact enzyme.
      Title: The N-terminal domain of the Escherichia coli PriA helicase contains both the DNA- and nucleotide-binding sites. Energetics of domain--DNA interactions and allosteric effect of the nucleotide cofactors.
    Submit: New GeneRIF Correction See all GeneRIFs (18)

    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 3'-5' DNA helicase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 3'-5' DNA helicase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA helicase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables helicase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables helicase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in DNA duplex unwinding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA recombination IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within DNA recombination IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in DNA replication IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within DNA replication IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in DNA replication initiation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within DNA replication initiation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in DNA replication, synthesis of primer IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA replication, synthesis of primer NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in DNA unwinding involved in DNA replication IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within DNA unwinding involved in DNA replication IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in DNA unwinding involved in DNA replication IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA unwinding involved in DNA replication NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within DNA-templated DNA replication IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in double-strand break repair IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within double-strand break repair IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within plasmid maintenance IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in replication fork processing NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within response to antibiotic IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within response to gamma radiation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of DnaB-DnaC-DnaT-PriA-PriB complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    part_of DnaB-DnaC-DnaT-PriA-PriC complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    part_of primosome complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of primosome complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    primosomal protein N'

    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
      4124612..4126810 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418370.1 primosomal protein N' [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418370.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7EJN4
      Conserved Domains (1) summary
      PRK05580
      Location:1 → 731
      PRK05580; primosome assembly protein PriA; Validated
    Nucleotide Protein
    Heading Accession and Version

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