Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Regulation of rtt107 recruitment to stalled DNA replication forks by the cullin rtt101 and the rtt109 acetyltransferase.

Molecular biology of the cell - 1 Jan 2008

Roberts Tania M, Zaidi Iram Waris, Vaisica Jessica A, Peter Matthias, Brown Grant W

Abstract excerpt

RTT107 (ESC4, YHR154W) encodes a BRCA1 C-terminal domain protein that is important for recovery from DNA damage during S phase. Rtt107 is a substrate of the checkpoint kinase Mec1, and it forms complexes with DNA repair enzymes, including the nuclease subunit Slx4, but the role of Rtt107 in the D...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylation
Share to Chromatin
Share to Cullin Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histone Acetyltransferases

Share to Lysine

Share to Methyl Methanesulfonate

Share to Replication Origin

Share to Suppression, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 17978089
DOI: 10.1091/mbc.e07-09-0961
PMCID: PMC2174167

Genes

BRCA1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17978089-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of rtt107 recruitment to stalled DNA replication forks by the cullin rtt101 and the rtt109 acetyltransferase.PMID 17978089Read ↗

Loss of H3 K79 trimethylation leads to suppression of Rtt107-dependent DNA damage sensitivity through the translesion synthesis pathway.Semantic proximity Read ↗

Rtt107 is required for recruitment of the SMC5/6 complex to DNA double strand breaks.Semantic proximity Read ↗

DNA-repair scaffolds dampen checkpoint signalling by counteracting the adaptor Rad9.Semantic proximity Read ↗

The Ddc1-Mec3-Rad17 sliding clamp regulates histone-histone chaperone interactions and DNA replication-coupled nucleosome assembly in budding yeast.Semantic proximity Read ↗

Rtt107 BRCT domains act as a targeting module in the DNA damage response.Semantic proximity Read ↗

Rtt107 Is a Multi-functional Scaffold Supporting Replication Progression with Partner SUMO and Ubiquitin Ligases.Semantic proximity Read ↗

The Replisome-Coupled E3 Ubiquitin Ligase Rtt101Mms22 Counteracts Mrc1 Function to Tolerate Genotoxic Stress.Semantic proximity Read ↗

Slx4 and Rtt107 control checkpoint signalling and DNA resection at double-strand breaks.Semantic proximity Read ↗

Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56.Semantic proximity Read ↗

Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication.Semantic proximity Read ↗

Rtt107 cooperates with Rad55 to limit specific types of genome instability in Saccharomyces cerevisiae.Semantic proximity Read ↗

Histone H3K56 acetylation, CAF1, and Rtt106 coordinate nucleosome assembly and stability of advancing replication forks.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.