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prfB peptide chain release factor RF2 [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947369, updated on 4-Feb-2026
Official Symbol
prfB
Official Full Name
peptide chain release factor RF2
Primary source
ECOCYC:EG10762
Locus tag
b2891
See related
ASAP:ABE-0009488
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK2886; supK
Summary
The ribosome changes reading frame after codon 25. [More information is available at EcoGene: EG10762]. Release factor 2 (RF2) 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: EG10762].
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Sequence:
NC_000913.3 (3035184..3036282, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene isopentenyl-diphosphate Delta-isomerase Neighboring gene lysine--tRNA ligase Neighboring gene ssDNA-specific exonuclease RecJ Neighboring gene protein disulfide isomerase DsbC

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. A computational model for reading frame maintenance. Ponnala L, et al. Conf Proc IEEE Eng Med Biol Soc, 2006. PMID 17946637
  2. Maintaining the ribosomal reading frame: the influence of the E site during translational regulation of release factor 2. Márquez V, et al. Cell, 2004 Jul 9. PMID 15242643
  3. Analysis of effects of tRNA:message stability on frameshift frequency at the Escherichia coli RF2 programmed frameshift site. Curran JF. Nucleic Acids Res, 1993 Apr 25. PMID 8493101, Free PMC Article
  4. Comparative characterization of release factor RF-3 genes of Escherichia coli, Salmonella typhimurium, and Dichelobacter nodosus. Kawazu Y, et al. J Bacteriol, 1995 Oct. PMID 7559341, Free PMC Article
  5. Enhancement of +1 frameshift by polyamines during translation of polypeptide release factor 2 in Escherichia coli. Higashi K, et al. J Biol Chem, 2006 Apr 7. PMID 16476727

See all (78) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Structural basis of l-tryptophan-dependent inhibition of release factor 2 by the TnaC arrest peptide.
    Title: Structural basis of l-tryptophan-dependent inhibition of release factor 2 by the TnaC arrest peptide.
  2. Molecular determinants of release factor 2 for ArfA-mediated ribosome rescue.
    Title: Molecular determinants of release factor 2 for ArfA-mediated ribosome rescue.
  3. In translation termination, the catalytic GGQ loop of RF2 is rearranged into a long beta-hairpin that plugs the peptide tunnel, biasing a nascent protein toward the ribosome exit.
    Title: Extensive ribosome and RF2 rearrangements during translation termination.
  4. 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.
  5. 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.
  6. 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.
  7. The structures demonstrate how ArfA 'senses' the vacant mRNA tunnel and activates RF2 to mediate peptide release without a stop codon, allowing stalled ribosomes to be recycled.
    Title: Mechanism of ribosome rescue by ArfA and RF2.
  8. The authors characterized the ArfA pathway of non-productive translation complexe resolution in vitro and identified RF2 as a factor that cooperates with ArfA to hydrolyse peptidyl-tRNAs located in the P-site of the stalled ribosome.
    Title: ArfA recruits release factor 2 to rescue stalled ribosomes by peptidyl-tRNA hydrolysis in Escherichia coli.
  9. RF2 binds to stalled ribosomes only in the presence of ArfA, demonstrating that ArfA recruits RF2 into the A site of the ribosome to facilitate peptidyl-tRNA hydrolysis.
    Title: ArfA recruits RF2 into stalled ribosomes.
  10. Mutations at the two positions on 23S rRNA did not affect aminoacyl-tRNA (aa-tRNA) accommodation, peptide bond formation, or the fidelity of aa-tRNA selection, but impaired RF2-catalyzed peptide release.
    Title: Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination.
Submit: New GeneRIF Correction See all GeneRIFs (16)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables translation release factor activity, codon specific IBA
Inferred from Biological aspect of Ancestor
more info
  
Process Evidence Code Pubs
involved_in translational termination IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
Preferred Names
peptide chain release factor RF2

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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
    3035184..3036282 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417367.1 peptide chain release factor RF2

    See identical proteins and their annotated locations for NP_417367.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    A8A432
    UniProtKB/TrEMBL
    A0A418GJ44, A0A7A7FUM9, A0A8S7CIS2
    Conserved Domains (1) summary
    PRK00578
    Location:3 → 365
    prfB; peptide chain release factor 2; Validated
Nucleotide Protein
Heading Accession and Version

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