YKU80 ATP-dependent DNA helicase YKU80 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: YKU80
Official Full Name: ATP-dependent DNA helicase YKU80
Primary source: SGD:S000004712
Locus tag: YMR106C
See related: AllianceGenome:SGD:S000004712; FungiDB:YMR106C; VEuPathDB:YMR106C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: HDF2
Summary: Enables telomerase RNA binding activity and telomeric DNA binding activity. Involved in several processes, including DNA metabolic process; establishment of protein-containing complex localization to telomere; and subtelomeric heterochromatin formation. Located in chromosome, telomeric region. Part of Ku70:Ku80 complex. Human ortholog(s) of this gene implicated in chronic obstructive pulmonary disease; multiple myeloma; and rectum cancer. Orthologous to human XRCC5 (X-ray repair cross complementing 5). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See YKU80 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (478301..480190, complement)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Suppression of telomere capping defects of Saccharomyces cerevisiae yku70 and yku80 mutants by telomerase.
Title: Suppression of telomere capping defects of Saccharomyces cerevisiae yku70 and yku80 mutants by telomerase.
CDK-mediated Yku80 Phosphorylation Regulates the Balance Between Non-homologous End Joining (NHEJ) and Homologous Directed Recombination (HDR).
Title: CDK-mediated Yku80 Phosphorylation Regulates the Balance Between Non-homologous End Joining (NHEJ) and Homologous Directed Recombination (HDR).
DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 becomes a suitable substrate for long-range 5'-3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends.
Title: A DNA nick at Ku-blocked double-strand break ends serves as an entry site for exonuclease 1 (Exo1) or Sgs1-Dna2 in long-range DNA end resection.
the yKu-distal portion of telomeres is bound by Rap1, which in turn reduces the potential for yKu(Yku80 and Yku70 )to mediate NHEJ. These results thus propose a solution to a long-standing conundrum, namely how to accommodate the apparently conflicting functions of Ku on telomeres.
Title: Ku Binding on Telomeres Occurs at Sites Distal from the Physical Chromosome Ends.
The authors show that Sir4 - a previously identified Ku-binding protein that is a component of telomeric silent chromatin - is required for Ku-mediated telomere lengthening and telomerase recruitment.
Title: The Ku subunit of telomerase binds Sir4 to recruit telomerase to lengthen telomeres in S. cerevisiae.
Deletion of Est1 has a much greater impact on telomere lengthening in the presence of a Cdc13-Est2 fusion than deletion of YKU80, suggesting that any contribution that Ku may have in telomerase activation is minor compared to that of Est1.
Title: The principal role of Ku in telomere length maintenance is promotion of Est1 association with telomeres.
The TORC1 signal is transduced by the Gln3/Gat1/Ure2 pathway, which controls the levels of the Ku heterodimer, a telomere regulator.
Title: Tor complex 1 controls telomere length by affecting the level of Ku.
These findings contradict the recruitment model of Ku binding both DNA and RNA simultaneously and lead to a new model for the mechanism by which Ku's interaction with TLC1 RNA contributes to telomerase recruitment.
Title: Mutually exclusive binding of telomerase RNA and DNA by Ku alters telomerase recruitment model.
Ku must load directly onto the chromosome end in order to mediate its telomeric functions
Title: Ku must load directly onto the chromosome end in order to mediate its telomeric functions.
The effect of Ku on telomere replication time is mediated by telomere length but is independent of histone tail acetylation. [YKU80]
Title: The effect of Ku on telomere replication time is mediated by telomere length but is independent of histone tail acetylation.

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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 SGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent H2AZ histone chaperone activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent H3-H4 histone complex chaperone 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 clamp loader activity	IEA Inferred from Electronic Annotation more info
enables chromatin extrusion motor activity	IEA Inferred from Electronic Annotation more info
enables cohesin loader activity	IEA Inferred from Electronic Annotation more info
enables damaged DNA binding	IEA Inferred from Electronic Annotation more info
contributes_to double-stranded DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables double-stranded DNA helicase activity	IEA Inferred from Electronic Annotation more info
enables forked DNA-dependent helicase activity	IEA Inferred from Electronic Annotation more info
enables four-way junction helicase activity	IEA Inferred from Electronic Annotation more info
enables helicase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables single-stranded 3'-5' DNA helicase activity	IEA Inferred from Electronic Annotation more info
enables telomerase RNA binding	IDA Inferred from Direct Assay more info	PubMed
enables telomeric DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables telomeric DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables telomeric DNA 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	IEA Inferred from Electronic Annotation more info
involved_in DNA repair	IEA Inferred from Electronic Annotation more info
involved_in chromatin looping	IEA Inferred from Electronic Annotation more info
involved_in chromatin organization	IDA Inferred from Direct Assay more info	PubMed
involved_in donor selection	IDA Inferred from Direct Assay more info	PubMed
involved_in donor selection	IGI Inferred from Genetic Interaction more info	PubMed
involved_in donor selection	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in double-strand break repair via homologous recombination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in double-strand break repair via nonhomologous end joining	IBA Inferred from Biological aspect of Ancestor more info
involved_in double-strand break repair via nonhomologous end joining	IEA Inferred from Electronic Annotation more info
involved_in double-strand break repair via nonhomologous end joining	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in establishment of protein-containing complex localization to telomere	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization to chromosome	IGI Inferred from Genetic Interaction more info	PubMed
involved_in subtelomeric heterochromatin formation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in telomere maintenance	IBA Inferred from Biological aspect of Ancestor more info
involved_in telomere maintenance	IEA Inferred from Electronic Annotation more info
involved_in telomere maintenance	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of Ku70:Ku80 complex	IBA Inferred from Biological aspect of Ancestor more info
part_of Ku70:Ku80 complex	IDA Inferred from Direct Assay more info	PubMed
part_of Ku70:Ku80 complex	IEA Inferred from Electronic Annotation more info
located_in chromosome	IEA Inferred from Electronic Annotation more info
located_in chromosome, telomeric region	IEA Inferred from Electronic Annotation more info
located_in chromosome, telomeric region	IMP Inferred from Mutant Phenotype more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: ATP-dependent DNA helicase YKU80

NP_013824.1

EC 3.6.4.12

Subunit of telomeric Ku complex (Yku70p-Yku80p); involved in telomere length maintenance, structure and telomere position effect; required for localization of telomerase ribonucleoprotein via interaction with TLC1 guide RNA; relocates to sites of double-strand cleavage to promote nonhomologous end joining during DSB repair; colocalizes with quiescent cell telomere hyperclusters

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001145.3 Reference assembly

Range

478301..480190 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182606.1 → NP_013824.1 TPA: ATP-dependent DNA helicase YKU80 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013824.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VZS9, Q04437, Q0P737, Q0P738, Q0P741, Q0P749

UniProtKB/TrEMBL

B3LLZ7, C7GVE3, C8ZEV9, N1P0B5

Conserved Domains (2) summary

cd00873
Location:244 → 583

KU80; Ku-core domain, Ku80 subfamily; Ku80 is a subunit of the Ku protein, which plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, and V(D)J recombination. The mechanism underlying the ...

cl00057
Location:5 → 232

vWFA; Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of ...