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Chuanbing Bian,
Chao Xu,
Jianbin Ruan,
Kenneth K Lee,
Tara L Burke,
Wolfram Tempel,
Dalia Barsyte,
Jing Li,
Minhao Wu,
Bo O Zhou,
Brian E Fleharty,
Ariel Paulson,
Abdellah Allali-Hassani,
Jin-Qiu Zhou, Georges Mer,
Patrick A Grant,
Jerry L Workman,
Jianye Zang,
Jinrong Min
[show abstract]
[hide abstract]
ABSTRACT: The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex is an important chromatin modifying complex that can both acetylate and deubiquitinate histones. Sgf29 is a novel component of the SAGA complex. Here, we report the crystal structures of the tandem Tudor domains of Saccharomyces cerevisiae and human Sgf29 and their complexes with H3K4me2 and H3K4me3 peptides, respectively, and show that Sgf29 selectively binds H3K4me2/3 marks. Our crystal structures reveal that Sgf29 harbours unique tandem Tudor domains in its C-terminus. The tandem Tudor domains in Sgf29 tightly pack against each other face-to-face with each Tudor domain harbouring a negatively charged pocket accommodating the first residue alanine and methylated K4 residue of histone H3, respectively. The H3A1 and K4me3 binding pockets and the limited binding cleft length between these two binding pockets are the structural determinants in conferring the ability of Sgf29 to selectively recognize H3K4me2/3. Our 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 Sgf29 in gene regulation.
The EMBO Journal 06/2011; 30(14):2829-42. · 9.20 Impact Factor
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Chuanbing Bian,
Chao Xu,
Jianbin Ruan,
Kenneth K Lee,
Tara L Burke,
Wolfram Tempel,
Dalia Barsyte,
Jing Li,
Minhao Wu,
Bo O Zhou,
Brian E Fleharty,
Ariel Paulson,
Abdellah Allali-Hassani,
Jin-Qiu Zhou, Georges Mer,
Patrick A Grant,
Jerry L Workman,
Jianye Zang,
Jinrong Min
[show abstract]
[hide abstract]
ABSTRACT: The SAGA (Spt–Ada–Gcn5 acetyltransferase) complex is an important chromatin modifying complex that can both acetylate and deubiquitinate histones. Sgf29 is a novel component of the SAGA complex. Here, we report the crystal structures of the tandem Tudor domains of
The EMBO Journal 06/2011; 30(14):2829-2842. · 9.20 Impact Factor
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[show abstract]
[hide abstract]
ABSTRACT: Elongin is a transcription elongation factor that stimulates the rate of elongation by suppressing transient pausing by RNA polymerase II at many sites along the DNA. It is heterotrimeric in mammals, consisting of elongins A, B and C subunits, and bears overall similarity to a class of E3 ubiquitin ligases known as SCF (Skp1-Cdc53 (cullin)-F-box) complexes. A subcomplex of elongins B and C is a target for negative regulation by the von Hippel-Lindau (VHL) tumor-suppressor protein. Elongin C from Saccharomyces cerevisiae, Elc1, exhibits high sequence similarity to mammalian elongin C. Using NMR spectroscopy we have determined the three-dimensional structure of Elc1 in complex with a human VHL peptide, VHL(157–171), representing the major Elc1 binding site. The bound VHL peptide is entirely helical. Elc1 utilizes two C-terminal helices and an intervening loop to form a binding groove that fits VHL(157–171). Chemical shift perturbation and dynamics analyses reveal that a global conformational change accompanies Elc1/VHL(157–171) complex formation. Moreover, the disappearance of conformational exchange phenomena on the microsecond to millisecond time scale within Elc1 upon VHL peptide binding suggests a role for slow internal motions in ligand recognition.
Journal of Molecular Biology 10/2001; · 4.00 Impact Factor
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Journal of Biomolecular NMR 05/2000; 17(2):179-180. · 3.61 Impact Factor
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01/1998;
