Richard S. Jones
Southern Methodist University
25 Papers
482 Citations
Richard S. Jones is an academic researcher from Southern Methodist University. The author has contributed to research in topics: Polycomb-group proteins & Histone methyltransferase. The author has an hindex of 18, co-authored 24 publications.
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Papers
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Ru Cao,Liangjun Wang,Hengbin Wang,Li Xia,Hediye Erdjument-Bromage,Paul Tempst,Richard S. Jones,Yi Zhang +7 more
TL;DR: The purification and characterization of an EED-EZH2 complex, the human counterpart of the Drosophila ESC-E(Z) complex, is reported, and it is demonstrated that the complex specifically methylates nucleosomal histone H3 at lysine 27 (H3-K27).
3.9K
Role of histone H2A ubiquitination in Polycomb silencing
Hengbin Wang,Liangjun Wang,Hediye Erdjument-Bromage,Miguel Vidal,Paul Tempst,Richard S. Jones,Yi Zhang +6 more
TL;DR: The purification and functional characterization of an E3 ubiquitin ligase complex that is specific for histone H2A is reported, and it is linked to Polycomb silencing, which is important in regulating chromatin dynamics and transcription.
1.8K
Hierarchical Recruitment of Polycomb Group Silencing Complexes
TL;DR: Evidence is provided for the sequential binding of PcG proteins at a Polycomb response element (PRE) in proliferating cells in which the sequence-specific DNA binding Pho and Phol proteins directly recruit E(z)-containing complexes, which in turn methylate histone H3 at lysine 27 (H3mK27).
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The Drosophila Enhancer of zeste gene encodes a chromosomal protein: examination of wild-type and mutant protein distribution
E.A. Carrington,Richard S. Jones +1 more
TL;DR: The in vivo distribution of the E(Z) protein is described and it is shown to be ubiquitously present in embryonic and larval nuclei and the sequences of one null and three temperature-sensitive E(z) alleles are presented.
137
Polycomblike PHD fingers mediate conserved interaction with enhancer of zeste protein.
TL;DR: PCL·E(Z) interaction is shown to be mediated by the plant homeodomain fingers domain of PCL, providing evidence that this motif can act as an independent protein interaction domain, and the possibility that PCL may either be a subunit of a subset of ESC·E (Z) complexes or a sub unit of a separate complex that interacts with ESC· E( Z) complexes.
125