Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex

Dan Su; Qi Hu; Hui Zhou; James R. Thompson; Rui Ming Xu; Zhiguo Zhang; Georges Mer

doi:10.1074/jbc.C111.220715

Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex

Dan Su, Qi Hu, Hui Zhou, James R. Thompson, Rui Ming Xu, Zhiguo Zhang, Georges Mer

Research output: Contribution to journal › Article › peer-review

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Abstract

The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)₂ tetramers. To investigate this activation mechanism, we determined x-ray structures of full-length Vps75 in complex with full-length Rtt109 in two crystal forms. Both structures show similar asymmetric assemblies of a Vps75 dimer bound to an Rtt109 monomer. In the Vps75-Rtt109 complexes, the catalytic site of Rtt109 is confined to an enclosed space that can accommodate the N-terminal tail of histone H3 in (H3-H4)₂. Investigation of Vps75-Rtt109-(H3-H4)₂ and Vps75-(H3-H4)₂ complexes by NMR spectroscopy-probed hydrogen/deuterium exchange suggests that Vps75 guides histone H3 in the catalytic enclosure. These findings clarify the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109.

Original language	English (US)
Pages (from-to)	15625-15629
Number of pages	5
Journal	Journal of Biological Chemistry
Volume	286
Issue number	18
DOIs	https://doi.org/10.1074/jbc.C111.220715
State	Published - May 6 2011
Externally published	Yes

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title = "Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex",

abstract = "The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)2 tetramers. To investigate this activation mechanism, we determined x-ray structures of full-length Vps75 in complex with full-length Rtt109 in two crystal forms. Both structures show similar asymmetric assemblies of a Vps75 dimer bound to an Rtt109 monomer. In the Vps75-Rtt109 complexes, the catalytic site of Rtt109 is confined to an enclosed space that can accommodate the N-terminal tail of histone H3 in (H3-H4)2. Investigation of Vps75-Rtt109-(H3-H4)2 and Vps75-(H3-H4)2 complexes by NMR spectroscopy-probed hydrogen/deuterium exchange suggests that Vps75 guides histone H3 in the catalytic enclosure. These findings clarify the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109.",

author = "Dan Su and Qi Hu and Hui Zhou and Thompson, {James R.} and Xu, {Rui Ming} and Zhiguo Zhang and Georges Mer",

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T1 - Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex

AU - Su, Dan

AU - Hu, Qi

AU - Zhou, Hui

AU - Thompson, James R.

AU - Xu, Rui Ming

AU - Zhang, Zhiguo

AU - Mer, Georges

PY - 2011/5/6

Y1 - 2011/5/6

N2 - The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)2 tetramers. To investigate this activation mechanism, we determined x-ray structures of full-length Vps75 in complex with full-length Rtt109 in two crystal forms. Both structures show similar asymmetric assemblies of a Vps75 dimer bound to an Rtt109 monomer. In the Vps75-Rtt109 complexes, the catalytic site of Rtt109 is confined to an enclosed space that can accommodate the N-terminal tail of histone H3 in (H3-H4)2. Investigation of Vps75-Rtt109-(H3-H4)2 and Vps75-(H3-H4)2 complexes by NMR spectroscopy-probed hydrogen/deuterium exchange suggests that Vps75 guides histone H3 in the catalytic enclosure. These findings clarify the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109.

AB - The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)2 tetramers. To investigate this activation mechanism, we determined x-ray structures of full-length Vps75 in complex with full-length Rtt109 in two crystal forms. Both structures show similar asymmetric assemblies of a Vps75 dimer bound to an Rtt109 monomer. In the Vps75-Rtt109 complexes, the catalytic site of Rtt109 is confined to an enclosed space that can accommodate the N-terminal tail of histone H3 in (H3-H4)2. Investigation of Vps75-Rtt109-(H3-H4)2 and Vps75-(H3-H4)2 complexes by NMR spectroscopy-probed hydrogen/deuterium exchange suggests that Vps75 guides histone H3 in the catalytic enclosure. These findings clarify the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109.

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JO - Journal of Biological Chemistry

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Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex

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