ArticleProceedings of the National Academy of Sciences of the United States of America2012
Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Mechanism of ASF1 engagement by CDAN1.Nature communications · 2025Article
- CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply.Nature communications · 2025Article
- Mechanism of ASF1 Inhibition by CDAN1.bioRxiv : the preprint server for biology · 2024Article
- Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry.Nature communications · 2022Article
- Review
- Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.Nucleic acids research · 2018Article
- Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017Review
- Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair.Genes & development · 2016Article
- Replisome function during replicative stress is modulated by histone h3 lysine 56 acetylation through Ctf4.Genetics · 2015Article
- ATR checkpoint kinase and CRL1βTRCP collaborate to degrade ASF1a and thus repress genes overlapping with clusters of stalled replication forks.Genes & development · 2014Article
- Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication.Nature communications · 2014Article
- ANTI-SILENCING FUNCTION1 proteins are involved in ultraviolet-induced DNA damage repair and are cell cycle regulated by E2F transcription factors in Arabidopsis.Plant physiology · 2013Article
- The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylation.Eukaryotic cell · 2013Article
- The C terminus of the histone chaperone Asf1 cross-links to histone H3 in yeast and promotes interaction with histones H3 and H4.Molecular and cellular biology · 2013Article
- CAF-1-induced oligomerization of histones H3/H4 and mutually exclusive interactions with Asf1 guide H3/H4 transitions among histone chaperones and DNA.Nucleic acids research · 2012Article
- Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1.Nucleus (Austin, Tex.)Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The histone chaperone Asf1 and the checkpoint kinase Rad53 are found in a complex in budding yeast cells in the absence of genotoxic stress. Our data suggest that this complex involves at least three interaction sites. One site involves the H3-binding surface of Asf11 with an as yet undefined surface of Rad53. A second site is formed by the Rad53-FHA1 domain binding to Asf1-T(270) phosphorylated by casein kinase II. The third site involves the C-terminal 21 amino acids of Rad53 bound to the conserved Asf1 N-terminal domain. The structure of this site showed that the Rad53 C-terminus binds Asf1 in a remarkably similar manner to peptides derived from the histone cochaperones HirA and CAF-I. We call this binding motif, (R/K)R(I/A/V) (L/P), the AIP box for Asf1-Interacting Protein box. Furthermore, C-terminal Rad53-F(820) binds the same pocket of Asf1 as does histone H4-F(100). Thus Rad53 competes with histones H3-H4 and cochaperones HirA/CAF-I for binding to Asf1. Rad53 is phosphorylated and activated upon genotoxic stress. The Asf1-Rad53 complex dissociated when cells were treated with hydroxyurea but not methyl-methane-sulfonate, suggesting a regulation of the complex as a function of the stress. We identified a rad53 mutation that destabilized the Asf1-Rad53 complex and increased the viability of rad9 and rad24 mutants in conditions of genotoxic stress, suggesting that complex stability impacts the DNA damage response.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.