ArticleProceedings of the National Academy of Sciences of the United States of America2012
Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing.
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 30 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
30 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- Pluripotency state transition of embryonic stem cells requires the turnover of histone chaperone FACT on chromatin.iScience · 2024Article
- Opposing Roles of FACT for Euchromatin and Heterochromatin in Yeast.Biomolecules · 2023Review
- Histone modification inComputational and structural biotechnology journal · 2023Review
- SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes.Nature communications · 2022Article
- The box C/D snoRNP assembly factor Bcd1 interacts with the histone chaperone Rtt106 and controls its transcription dependent activity.Nature communications · 2021Article
- Cac1 WHD and PIP domains have distinct roles in replisome progression and genomic stability.Current genetics · 2021Article
- Transcription shapes genome-wide histone acetylation patterns.Nature communications · 2021Article
- The role of FACT in managing chromatin: disruption, assembly, or repair?Nucleic acids research · 2020Review
- Proteomic Analysis of Histones H2A/H2B and Variant Hv1 in Tetrahymena thermophila Reveals an Ancient Network of Chaperones.Molecular biology and evolution · 2019Article
- Article
- Identification of Elg1 interaction partners and effects on post-replication chromatin re-formation.PLoS genetics · 2018Article
- Rtt105 functions as a chaperone for replication protein A to preserve genome stability.The EMBO journal · 2018Article
- Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones.The Journal of biological chemistry · 2018Article
- Pivotal roles of PCNA loading and unloading in heterochromatin function.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.Nature communications · 2017Article
- Structure of the human histone chaperone FACT Spt16 N-terminal domain.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Crystal Structure of Human SSRP1 Middle Domain Reveals a Role in DNA Binding.Scientific reports · 2015Article
- Article
- Histone core modifications regulating nucleosome structure and dynamics.Nature reviews. Molecular cell biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The histone chaperone Rtt106 binds histone H3 acetylated at lysine 56 (H3K56ac) and facilitates nucleosome assembly during several molecular processes. Both the structural basis of this modification-specific recognition and how this recognition informs Rtt106 function are presently unclear. Guided by our crystal structure of Rtt106, we identified two regions on its double-pleckstrin homology domain architecture that mediated histone binding. When histone binding was compromised, Rtt106 localized properly to chromatin but failed to deliver H3K56ac, leading to replication and silencing defects. By mutating analogous regions in the structurally homologous chromatin-reorganizer Pob3, we revealed a conserved histone-binding function for a basic patch found on both proteins. In contrast, a loop connecting two β-strands was required for histone binding by Rtt106 but was dispensable for Pob3 function. Unlike Rtt106, Pob3 histone binding was modification-independent, implicating the loop of Rtt106 in H3K56ac-specific recognition in vivo. Our studies described the structural origins of Rtt106 function, identified a conserved histone-binding surface, and defined a critical role for Rtt106:H3K56ac-binding specificity in silencing and replication-coupled nucleosome turnover.
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.