S
Steven A. Jacobs
Researcher at University of Virginia Health System
Publications - 6
Citations - 2114
Steven A. Jacobs is an academic researcher from University of Virginia Health System. The author has contributed to research in topics: Chromodomain & Histone H3. The author has an hindex of 5, co-authored 5 publications receiving 2025 citations. Previous affiliations of Steven A. Jacobs include University of Virginia.
Papers
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Journal ArticleDOI
Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains
Wolfgang Fischle,Yanming Wang,Steven A. Jacobs,Youngchang Kim,C. David Allis,C. David Allis,Sepideh Khorasanizadeh +6 more
TL;DR: It is shown that the chromodomain proteins Polycomb (Pc) and HP1 (heterochromatin protein 1) are highly discriminatory for binding to these sites in vivo and in vitro, and a role for their Chromodomains in both target site binding and discrimination is indicated.
Journal ArticleDOI
Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail.
TL;DR: Structural, energetic, and mutational analyses of the complex between the Drosophila HP1 chromodomain and the histone H3 tail with a methyllysine at residue 9 suggest a role for cation-π and van der Waals interactions, with trimethylation slightly improving the binding affinity.
Journal ArticleDOI
The active site of the SET domain is constructed on a knot.
Steven A. Jacobs,Joel M. Harp,Srikripa Devarakonda,Youngchang Kim,Fraydoon Rastinejad,Sepideh Khorasanizadeh +5 more
TL;DR: A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain.
Journal ArticleDOI
Specificity of the Chromodomain Y Chromosome Family of Chromodomains for Lysine-methylated ARK(S/T) Motifs
Wolfgang Fischle,Wolfgang Fischle,Wolfgang Fischle,Henriette Franz,Steven A. Jacobs,C. David Allis,C. David Allis,Sepideh Khorasanizadeh +7 more
TL;DR: The studies underscore the significance of subtle sequence differences in a conserved signaling module for diverse epigenetic regulatory pathways and support the in vitro binding properties of the chromodomains, the full-length CDY family proteins exhibit substantial variability in chromatin localization.
Book ChapterDOI
Assays for the determination of structure and dynamics of the interaction of the chromodomain with histone peptides.
TL;DR: Several biophysical methods, including nuclear magnetic resonance (NMR), X-ray crystallography, fluorescence spectroscopy, and isothermal titration calorimetry (ITC), are successfully applied to study the specificities and affinities of the interactions of chromodomains with histone tails.