TY - JOUR
T1 - A SPOT on the chromatin landscape? Histone peptide arrays as a tool for epigenetic research
AU - Nady, Nataliya
AU - Min, Jinrong
AU - Kareta, Michael S.
AU - Chédin, Frédéric
AU - Arrowsmith, Cheryl H.
N1 - Funding Information:
We apologize to all researchers whose important contributions could not be cited owing to space limitations. We thank G. Brothers and N. Warner, a post-doctoral fellow in the A. Pawson laboratory, for initial technical assistance with the peptide synthesizer, and A. Schuetz for providing purified WDR5. We are grateful to G. Brothers and P. Cheung for fruitful discussions and critical reading of the manuscript. This research was supported by the Canadian Cancer Society, the Canada Research Chairs program (to C.H.A.) and the Structural Genomics Consortium, a registered charity (number 1097737) that receives funds from the Canadian Institutes for Health Research, the Canadian Foundation for Innovation, Genome Canada through the Ontario Genomics Institute, GlaxoSmithKline, Karolinska Institutet, the Knut and Alice Wallenberg Foundation, the Ontario Innovation Trust, the Ontario Ministry for Research and Innovation, Merck and Co., the Novartis Research Foundation, the Swedish Foundation for Strategic Research, Vinnova (the Swedish Governmental Agency for Innovation Systems) and the Wellcome Trust. M.S.K. was supported by the UC Davis CIRM Training Grant with additional support from a Basil O’Connor Starter Scholar Award from the March of Dimes Foundation (to F.C.).
PY - 2008/7
Y1 - 2008/7
N2 - Post-translational modifications of histones serve as docking sites and signals for effector proteins and chromatin-remodeling enzymes, thereby influencing many fundamental cellular processes. Nevertheless, there are huge gaps in the knowledge of which proteins read and write the 'histone code'. Several techniques have been used to decipher complex histone-modification patterns. However, none is entirely satisfactory owing to the inherent limitations of in vitro studies of histones, such as deficits in the knowledge of the proteins involved, and the associated difficulties in the consistent and quantitative generation of histone marks. An alternative technique that could prove to be a useful tool in the study of the histone code is the use of synthetic peptide arrays (SPOT blot analysis) as a screening approach to characterize macromolecules that interact with specific covalent modifications of histone tails.
AB - Post-translational modifications of histones serve as docking sites and signals for effector proteins and chromatin-remodeling enzymes, thereby influencing many fundamental cellular processes. Nevertheless, there are huge gaps in the knowledge of which proteins read and write the 'histone code'. Several techniques have been used to decipher complex histone-modification patterns. However, none is entirely satisfactory owing to the inherent limitations of in vitro studies of histones, such as deficits in the knowledge of the proteins involved, and the associated difficulties in the consistent and quantitative generation of histone marks. An alternative technique that could prove to be a useful tool in the study of the histone code is the use of synthetic peptide arrays (SPOT blot analysis) as a screening approach to characterize macromolecules that interact with specific covalent modifications of histone tails.
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U2 - 10.1016/j.tibs.2008.04.014
DO - 10.1016/j.tibs.2008.04.014
M3 - Article
C2 - 18538573
AN - SCOPUS:46149116301
SN - 0376-5067
VL - 33
SP - 305
EP - 313
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 7
ER -