Genetically directing epsilon-N, N-dimethyl-L-lysine in recombinant histones

Duy P. Nguyen; Maria M. Garcia Alai; Satpal Virdee; Jason W. Chin

doi:10.1016/j.chembiol.2010.07.013

Genetically directing epsilon-N, N-dimethyl-L-lysine in recombinant histones

Duy P. Nguyen
, Maria M. Garcia Alai
, Satpal Virdee
, Jason W. Chin

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

83 Citations (Scopus)

Abstract

A molecular understanding of the biological phenomena orchestrated by lysine NE-methylation is impeded by the challenge of producing site-specifically and quantitatively methylated histones Here, we report a general method that combines genetic code expansion and chemoselective reactions, for the quantitative, site-specific installation of dimethyllysine in recombinant histones We demonstrate the utility of our method by preparing H3K9me2 and show that this modified histone is specifically recognized by heterochromatin protein 1 beta Extensions of the strategy reported here will allow a range of chemoselective reactions (which have been used for residue-selective, but not site-selective protein modification) to be leveraged for site-specific protein modification

Original language	English
Pages (from-to)	1072-1076
Number of pages	5
Journal	Chemistry & Biology
Volume	17
Issue number	10
DOIs	https://doi.org/10.1016/j.chembiol.2010.07.013
Publication status	Published - 29 Oct 2010

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title = "Genetically directing epsilon-N, N-dimethyl-L-lysine in recombinant histones",

abstract = "A molecular understanding of the biological phenomena orchestrated by lysine NE-methylation is impeded by the challenge of producing site-specifically and quantitatively methylated histones Here, we report a general method that combines genetic code expansion and chemoselective reactions, for the quantitative, site-specific installation of dimethyllysine in recombinant histones We demonstrate the utility of our method by preparing H3K9me2 and show that this modified histone is specifically recognized by heterochromatin protein 1 beta Extensions of the strategy reported here will allow a range of chemoselective reactions (which have been used for residue-selective, but not site-selective protein modification) to be leveraged for site-specific protein modification",

author = "Nguyen, \{Duy P.\} and Alai, \{Maria M. Garcia\} and Satpal Virdee and Chin, \{Jason W.\}",

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doi = "10.1016/j.chembiol.2010.07.013",

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T1 - Genetically directing epsilon-N, N-dimethyl-L-lysine in recombinant histones

AU - Nguyen, Duy P.

AU - Alai, Maria M. Garcia

AU - Virdee, Satpal

AU - Chin, Jason W.

PY - 2010/10/29

Y1 - 2010/10/29

N2 - A molecular understanding of the biological phenomena orchestrated by lysine NE-methylation is impeded by the challenge of producing site-specifically and quantitatively methylated histones Here, we report a general method that combines genetic code expansion and chemoselective reactions, for the quantitative, site-specific installation of dimethyllysine in recombinant histones We demonstrate the utility of our method by preparing H3K9me2 and show that this modified histone is specifically recognized by heterochromatin protein 1 beta Extensions of the strategy reported here will allow a range of chemoselective reactions (which have been used for residue-selective, but not site-selective protein modification) to be leveraged for site-specific protein modification

AB - A molecular understanding of the biological phenomena orchestrated by lysine NE-methylation is impeded by the challenge of producing site-specifically and quantitatively methylated histones Here, we report a general method that combines genetic code expansion and chemoselective reactions, for the quantitative, site-specific installation of dimethyllysine in recombinant histones We demonstrate the utility of our method by preparing H3K9me2 and show that this modified histone is specifically recognized by heterochromatin protein 1 beta Extensions of the strategy reported here will allow a range of chemoselective reactions (which have been used for residue-selective, but not site-selective protein modification) to be leveraged for site-specific protein modification

U2 - 10.1016/j.chembiol.2010.07.013

DO - 10.1016/j.chembiol.2010.07.013

M3 - Article

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SP - 1072

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JO - Chemistry & Biology

JF - Chemistry & Biology

IS - 10

ER -

Genetically directing epsilon-N, N-dimethyl-L-lysine in recombinant histones

Abstract

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