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 - Chedin, Frederic
AU - Arrowsmith, Cheryl H.
PY - 2008/7/1
Y1 - 2008/7/1
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
VL - 33
SP - 305
EP - 313
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
SN - 0376-5067
IS - 7
ER -