U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

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

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

Summary

Go to the top of the page Help
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].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
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

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

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

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

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

Go to the top of the page Help
Preferred Names
primosomal protein N'

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.