Perceiving the epigenetic landscape through histone readers
By C. Musselman, Marie-Eve Lalonde, J. Côté, Tatiana G. Kutateladze. Nature Structural &Molecular Biology, 2012
808 citations recorded by the source corpus.
Post-translational modifications (PTMs) of histones provide a fine-tuned mechanism for regulating chromatin structure and dynamics. PTMs can alter direct interactions between histones and DNA and serve as docking sites for protein effectors, or readers, of these PTMs. Binding of the readers recruits or stabilizes various components of the nuclear signaling machinery at specific genomic sites, mediating fundamental DNA-templated processes, including gene transcription and DNA recombination, replication and repair. In this review, we highlight the latest advances in characterizing histone-binding mechanisms and identifying new epigenetic readers and summarize the functional significance of PTM recognition.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/57571d30ef0175db56ed8e613a7878d3ed8d0d7d
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- B. O’Malley
- Brian D. Strahl
- Scott B. Rothbart
- Leah A. Gates
- Tatiana G. Kutateladze
- K. V. van Wely
- C. Foulds
- C. D. Allis
Citations in the corpus
- Interpreting thelanguage of histone and DNA modifications (2014, background): “Recent comprehensive reviews detail the structural properties of these and other identified histone reader domains and highlight the diverse biochemical implications of their interactions [33, 34].”
- A Unique pH-Dependent Recognition of Methylated Histone H3K4 by PPS and DIDO. (2017, background): “This value is in the range of binding affinities exhibited by the majority of epigenetic readers (Andrews et al., 2016; Musselman et al., 2012; Taverna et al., 2007).”
- Histone Marks in the 'Driver's Seat': Functional Roles in Steering the Transcription Cycle. (2017, background): “Epigenetic reader proteins have particular domains that interact with modified histone residues (reviewed in [6]).”
- Dido3 PHD modulates cell differentiation and division. (2013, neutral): “The PHD domain belongs to a large family of zinc fingers that recognize posttranslationally modified histone tails, including methylated lysine residues (Musselman and Kutateladze, 2011; Musselman et al., 2012); however, its role in the diverse activities of Dido3 remains unclear.”