dnaN beta sliding clamp [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: dnaN
Official Full Name: beta sliding clamp
Primary source: ECOCYC:EG10242
Locus tag: b3701
See related: ASAP:ABE-0012098
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: ECK3693
Summary: The beta subunit of DNA polymerase III dimerizes to form the sliding clamp that links the core polymerase to DNA and allows processive DNA replication. [More information is available at EcoCyc: EG10242].
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Genomic context

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Sequence:: NC_000913.3 (3881221..3882321, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Elevated Levels of the Escherichia coli nrdAB-Encoded Ribonucleotide Reductase Counteract the Toxicity Caused by an Increased Abundance of the beta Clamp.
Title: Elevated Levels of the Escherichia coli nrdAB-Encoded Ribonucleotide Reductase Counteract the Toxicity Caused by an Increased Abundance of the β Clamp.
The Mutant beta(E202K) Sliding Clamp Protein Impairs DNA Polymerase III Replication Activity.
Title: The Mutant β(E202K) Sliding Clamp Protein Impairs DNA Polymerase III Replication Activity.
In Bacillus subtilis, the interaction stimulates the endonuclease activity of MutL and it is critical for DNA mismatch repair. Conversely, disrupting the interaction between Escherichia coli MutL and the b-clamp only causes a mild mutator phenotype. Here, we determined the structures of the regulatory domains of E. coli and B. subtilis MutL bound to their respective b-clamps
Title: Binding of the regulatory domain of MutL to the sliding β-clamp is species specific.
Results demonstrate that the beta-clamp of the Escherichia coli replisome strongly inhibits nick translation on the DNA substrate. beta-clamp inhibits the strand displacement activity of Pol I by interfering with the interaction between the finger subdomain of Pol I and the downstream primer-template junction. beta-clamp stimulates the 5' exonuclease property of Pol I to cleave single nucleotides or shorter oligonucleo...
Title: Escherichia coli β-clamp slows down DNA polymerase I dependent nick translation while accelerating ligation.
structural and mutational analyses of the Hda-beta clamp complex indicate that the interaction of the beta clamp with Hda controls the ability of Hda to interact with DnaA.
Title: Dynamic assembly of Hda and the sliding clamp in the regulation of replication licensing.
The Escherichia coli beta clamp can simultaneously bind the replicative polymerase (Pol) III and the conserved Y-family Pol IV, enabling exchange of the two polymerases and rapid bypass of a Pol IV cognate lesion.
Title: Polymerase exchange on single DNA molecules reveals processivity clamp control of translesion synthesis.
A structural model of the alphaepsilontheta;:beta2 replicase complex reveals a compact, but still flexible, structure of the complex.
Title: Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, epsilon, θ and β reveals a highly flexible arrangement of the proofreading domain.
DNA polymerase III beta may stimulate the endonuclease activity of MutL through its direct interaction with the C-terminal domain of MutL.
Title: The endonuclease domain of MutL interacts with the β sliding clamp.
Escherichia coli cells with a point mutation in the dnaN gene causing the amino acid change Gly157 to Cys, were found to underinitiate replication and grow with a reduced origin and DNA concentration.
Title: The G157C mutation in the Escherichia coli sliding clamp specifically affects initiation of replication.
Study shows that the little finger domain of PolIV-beta interaction stabilizes the clamp-polymerase complex in vitro and is necessary for the access of PolIV to ongoing replication forks in vivo.
Title: Distinct beta-clamp interactions govern the activities of the Y family PolIV DNA polymerase.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables 3'-5' exonuclease activity	IEA Inferred from Electronic Annotation more info
enables DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables DNA-directed DNA polymerase activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
acts_upstream_of_or_within DNA damage response	IEP Inferred from Expression Pattern more info	PubMed
involved_in DNA replication	IEA Inferred from Electronic Annotation more info
involved_in DNA strand elongation involved in DNA replication	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within DNA strand elongation involved in DNA replication	IDA Inferred from Direct Assay more info	PubMed
involved_in DNA-templated DNA replication	NAS Non-traceable Author Statement more info	PubMed
acts_upstream_of_or_within bacterial-type DNA replication	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within error-prone translesion synthesis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of DNA-templated DNA replication initiation	NAS Non-traceable Author Statement more info	PubMed
involved_in regulation of DNA-templated DNA replication initiation	NAS Non-traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
part_of DNA polymerase III complex	IDA Inferred from Direct Assay more info	PubMed
part_of DNA polymerase III complex	IEA Inferred from Electronic Annotation more info
part_of DNA polymerase III complex	NAS Non-traceable Author Statement more info	PubMed
part_of Hda-beta clamp complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytoplasm	EXP Inferred from Experiment more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
part_of replication inhibiting complex	IPI Inferred from Physical Interaction more info	PubMed
part_of replisome	NAS Non-traceable Author Statement more info	PubMed