ArticleMolecular and cellular biology2013
The C terminus of the histone chaperone Asf1 cross-links to histone H3 in yeast and promotes interaction with histones H3 and H4.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Structure of the Hir histone chaperone complex.Molecular cell · 2024Article
- Article
- Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry.Nature communications · 2022Article
- Mitochondrial cytochrome c shot towards histone chaperone condensates in the nucleus.FEBS open bio · 2021Review
- Mild dyserythropoiesis and β-like globin gene expression imbalance due to the loss of histone chaperone ASF1B.Human genomics · 2020Article
- The replisome guides nucleosome assembly during DNA replication.Cell & bioscience · 2020Review
- Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.Nucleic acids research · 2019Article
- Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Journal of molecular biology · 2017Review
- Replisome function during replicative stress is modulated by histone h3 lysine 56 acetylation through Ctf4.Genetics · 2015Article
- Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication.Nature communications · 2014Article
- Characterization of two different Asf1 histone chaperones with distinct cellular localizations and functions in Trypanosoma brucei.Nucleic acids research · 2014Article
- An in vivo photo-cross-linking approach reveals a homodimerization domain of Aha1 in S. cerevisiae.PloS one · 2014Article
- Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1.Nucleus (Austin, Tex.)Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The central histone H3/H4 chaperone Asf1 comprises a highly conserved globular core and a divergent C-terminal tail. While the function and structure of the Asf1 core are well known, the function of the tail is less well understood. Here, we have explored the role of the yeast (yAsf1) and human (hAsf1a and hAsf1b) Asf1 tails in Saccharomyces cerevisiae. We show, using a photoreactive, unnatural amino acid, that Asf1 tail residue 210 cross-links to histone H3 in vivo and, further, that loss of C-terminal tail residues 211 to 279 weakens yAsf1-histone binding affinity in vitro nearly 200-fold. Via several yAsf1 C-terminal truncations and yeast-human chimeric proteins, we found that truncations at residue 210 increase transcriptional silencing and that the hAsf1a tail partially substitutes for full-length yAsf1 with respect to silencing but that full-length hAsf1b is a better overall substitute for full-length yAsf1. In addition, we show that the C-terminal tail of Asf1 is phosphorylated at T270 in yeast. Loss of this phosphorylation site does not prevent coimmunoprecipitation of yAsf1 and Rad53 from yeast extracts, whereas amino acid residue substitutions at the Asf1-histone H3/H4 interface do. Finally, we show that residue substitutions in yAsf1 near the CAF-1/HIRA interface also influence yAsf1's function in silencing.
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