CellStructureMech

DNA polymerase III, beta sliding clamp processivity factor complex

GO:0044775 · Other · Multiprotein complex · Proposed

A subcomplex of the DNA polymerase III holoenzyme which is responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. The complex is homodimeric in prokaryotes, and homotrimeric in other species. [GO:0044775]

Part of: DNA polymerase III complex (GO:0009360)

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

ComponentTypePart of / acts onGroundingGenesStoichiometryEssentialRole
DNA polymerase III beta subunitProteinpart ofReviewed label only (reviewed name; no accession asserted)dnaNtwo copies per prokaryotic clamp ringUNKNOWNRing-forming beta subunit that dimerizes to make the prokaryotic DNA polymerase III sliding clamp.
  • GO:0044775 GO:0044775 defines the beta sliding-clamp processivity factor complex as homodimeric in prokaryotes.
  • PMID:1349852 Kong et al. 1992 solved the E. coli DNA polymerase III beta subunit crystal structure and described a beta-subunit dimer forming a ring-shaped structure that can encircle duplex DNA.
  • UniProtKB:P0A988 UniProtKB P0A988 is the reviewed Escherichia coli K-12 dnaN entry for the beta sliding clamp.

Organism-specific protein examples

Named proteins in which each component's role was established, with the organism the evidence comes from. The component above is the taxon-agnostic family; these are the specific entries behind it.

DNA polymerase III beta subunit

AccessionProteinGeneOrganismEntry
UniProtKB:P0A988Beta sliding clampdnaNEscherichia coli K-12 (NCBITaxon:83333)REVIEWED
Role and evidence (1 reference)

Reviewed E. coli K-12 DnaN accession for the DNA polymerase III beta sliding-clamp subunit.

  • UniProtKB:P0A988 UniProtKB P0A988 is the reviewed Escherichia coli K-12 dnaN entry for the beta sliding clamp.

Canonical examples

Functions

Mechanism graphs

Beta sliding clamp tethers DNA polymerase III to DNA (FUNCTION)

The DnaN beta subunit dimer forms the beta sliding clamp that encircles duplex DNA and tethers the Pol III core during processive DNA replication.

SubjectPredicateObjectEvidence
DNA polymerase III beta subunitis part ofDNA polymerase III, beta sliding clamp processivity factor complex
  • PMID:1349852 Kong et al. 1992 reported that a dimer of the E. coli beta subunit forms a ring-shaped structure.
  • GO:0044775 GO:0044775 defines the beta sliding-clamp complex as homodimeric in prokaryotes.
DNA polymerase III, beta sliding clamp processivity factor complexencirclesduplex DNA
  • PMID:1349852 The E. coli beta-subunit dimer crystal structure forms a ring lined by alpha helices that can encircle duplex DNA.
DNA polymerase III, beta sliding clamp processivity factor complextethersDNA polymerase III, core complex
  • GO:0044775 GO:0044775 defines the beta sliding-clamp complex by its responsibility for tethering the catalytic subunit of DNA polymerase to DNA.
DNA polymerase III, beta sliding clamp processivity factor complexsupportsDNA replication
  • GO:0044775 GO:0044775 places the beta sliding clamp within the DNA polymerase III holoenzyme during high-speed DNA replication.
  • GO:0006260 GO:0006260 defines the DNA replication biological process.

Discussions

Evidence

Curation history

Source: data/structures/other/dna_polymerase_iii_beta_sliding_clamp_processivity_factor_complex.yaml