U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    prfA peptide chain release factor RF1 [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 949002, updated on 17-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    prfA
    Official Full Name
    peptide chain release factor RF1
    Primary source
    ECOCYC:EG10761
    Locus tag
    b1211
    See related
    ASAP:ABE-0004066
    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
    ECK1199; sueB; uar; ups?
    Summary
    Overexpression causes filamentous biofilm formation. [More information is available at EcoGene: EG10761]. Release factor 1 (RF1) is one of two class 1 codon-specific factors in Escherichia coli that facilitate the release of the growing polypeptide chain at stop codons. [More information is available at EcoCyc: EG10761].
    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 (1265012..1266094)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase Neighboring gene outer membrane lipoprotein LolB Neighboring gene glutamyl-tRNA reductase Neighboring gene protein-(glutamine-N(5)) methyltransferase Neighboring gene SirB family protein YchQ Neighboring gene transglutaminase-like/TPR repeat-containing protein

    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. Functional interaction between release factor one and P-site peptidyl-tRNA on the ribosome. Zhang S, et al. J Mol Biol, 1996 Aug 16. PMID 8757279
    2. A temperature-sensitive mutant of Escherichia coli that shows enhanced misreading of UAG/A and increased efficiency for some tRNA nonsense suppressors. Rydén SM, et al. Mol Gen Genet, 1984. PMID 6419024
    3. Effects of release factor context at UAA codons in Escherichia coli. Martin R, et al. J Bacteriol, 1988 Oct. PMID 3049546, Free PMC Article
    4. In vitro selection of RNA aptamers for the Escherichia coli release factor 1. Ogawa A, et al. Nucleic Acids Symp Ser (Oxf), 2005. PMID 17150737
    5. In vitro selection of RNA aptamer against Escherichia coli release factor 1. Sando S, et al. Bioorg Med Chem Lett, 2007 Mar 1. PMID 17188871

    See all (70) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Study used time-resolved cryo-EM to visualize transient compact forms of RF1 and RF2 at 3.5 and 4 A resolution, respectively, in the codon-recognizing ribosome complex on the native pathway. About 25% of complexes have RFs in the compact state at 24 ms reaction time, and within 60 ms virtually all ribosome-bound RFs are transformed to their extended forms.
      Title: The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy.
    2. Ribosome termination complexes that carry two factors, RF1-RF3 or RF2-RF3, are dynamic and fluctuate between non-rotated and rotated states, whereas each factor alone has its distinct signature on ribosome dynamics and conformation.
      Title: Dynamics of ribosomes and release factors during translation termination in E. coli.
    3. both RF1 binding and RF2 binding are sufficient to shift the population of posthydrolysis ribosome complexes from primarily the rotated to the nonrotated state only when a cognate stop codon is present in the A-site.
      Title: Operative Binding of Class I Release Factors and YaeJ Stabilizes the Ribosome in the Nonrotated State.
    4. Data show that peptide chain release factor RF-3 (RF3) hydrolyzes GTP and dissociates from the ribosome before peptide chain release factor RF-1 (RF1)dissociation.
      Title: Mechanism of Translation Termination: RF1 Dissociation Follows Dissociation of RF3 from the Ribosome.
    5. These results indicate that RF1 undergoes a large conformational change from a closed to an open form upon binding to the ribosome.
      Title: Ribosome Induces a Closed to Open Conformational Change in Release Factor 1.
    6. In a strain lacking RF-1, phosphoserine phosphatase, and where seven UAG codons residing in essential genes were converted to UAA, phosphoserine incorporation into GFP and WNK4 was significantly elevated
      Title: Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion.
    7. Release factor one is nonessential in Escherichia coli
      Title: Release factor one is nonessential in Escherichia coli.
    8. a conformational change within the RF1.ribosome complex that results in a more tightly bound state
      Title: Histidine 197 in release factor 1 is essential for a site binding and peptide release.
    9. Hypomodification of some tRNAs can suppress the Ts phenotype caused by the RF1 mutant.
      Title: Hypomodification of the wobble base in tRNAGlu, tRNALys, and tRNAGln suppresses the temperature-sensitive phenotype caused by mutant release factor 1.
    10. RF1 mutations strongly reduce the specific termination activity of RF1 at UAG codons, and lead to hypersensitivity to Kid and RelE toxins.
      Title: Novel Escherichia coli RF1 mutants with decreased translation termination activity and increased sensitivity to the cytotoxic effect of the bacterial toxins Kid and RelE.
    Submit: New GeneRIF Correction See all GeneRIFs (12)

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables ribosome binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables translation release factor activity, codon specific IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables translation release factor activity, codon specific IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in translational termination IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within translational termination IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    peptide chain release factor RF1

    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
      1265012..1266094
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415729.1 peptide chain release factor RF1 [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415729.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376M8P3, A0A418GSB5, A0A6C9QF94, A0A7A6MJY7
      Conserved Domains (1) summary
      PRK00591
      Location:2 → 358
      prfA; peptide chain release factor 1; 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.