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Structural Insights into Histone Demethylation by JMJD2 Family Members
Sited-directed mutagenesis in conjunction with demethylase activity assays allowed us to propose a molecular model for substrate selection by the JMJD2 histone dem methylase family. Expand
Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation
In vitro and in vivo functional assays show that Sgf29 recognizes methylated H3K4 to recruit the SAGA complex to its targets sites and mediates histone H3 acetylation, underscoring the importance of Sf29 in gene regulation. Expand
Interaction of JMJD6 with single-stranded RNA
The structures of JMJD6 with and without α-ketoglutarate revealed a novel substrate binding groove and two positively charged surfaces, which suggest that JMJD 6 may bind and modify single-stand RNA rather than the previously reported peptide substrates. Expand
Structural basis of the recognition of a methylated histone tail by JMJD2A
Structures of the JMJD2A catalytic core complexed with methylated H3K36 peptide substrates in the presence of Fe(II) and N-oxalylglycine are presented to provide insights into the mechanisms and specificity of histone demethylation. Expand
Mitotic Regulator Mis18β Interacts with and Specifies the Centromeric Assembly of Molecular Chaperone Holliday Junction Recognition Protein (HJURP)*
It is shown that human HJURP directly binds to Mis18β, a component of the Mis18 complex conserved in the eukaryotic kingdom, defining a novel molecular mechanism underlying the temporal regulation of CENP-A incorporation into the centromere by accurate Mis18 β-HJurP interaction. Expand
Structural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin Silencing*
The 2.5 Å crystal structure of the core domain of Rtt106p is reported, which adopts an unusual “double pleckstrin homology” domain architecture that represents a novel structural mode for histone chaperones. Expand
Crystal Structure of Human Vacuolar Protein Sorting Protein 29 Reveals a Phosphodiesterase/Nuclease-like Fold and Two Protein-Protein Interaction Sites*
HVps29p contains a metal-binding site that is very similar to the active sites of some proteins of the phosphodiesterase/nuclease protein family, indicating that hVPS29p may carry out chemically similar functions. Expand
Molecular basis for CENP-N recognition of CENP-A nucleosome on the human kinetochore
Spindlin‐1 recognizes methylations of K20 and R23 of histone H4 tail
Using methods combining cross‐linking, pull‐down assays, and stable isotope labeling by amino acids in cell culture with mass spectrometry, we identified that the Tudor domain‐containing proteinExpand
Solution NMR characterization of Sgf73(1-104) indicates that Zn ion is required to stabilize zinc finger motif.
Solution NMR and circular dichroism analysis of Sgf73(1-104) after zinc ion removal using chelation reagent EDTA (ethylene-diamine-tetraacetic acid) demonstrated that zinc ion was required to maintain stable conformation of the zinc finger motif. Expand