Influence of combinatorial histone modifications on antibody and effector protein recognition.

Influence of combinatorial histone modifications on antibody and effector protein recognition.
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DOI:
10.1016/j.cub.2010.11.058
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发表时间:
2011-01-11
期刊:
影响因子:
9.2
通讯作者:
Strahl, Brian D.
Strahl, Brian D.
中科院分区:
生物学1区
文献类型:
--
作者:
Fuchs, Stephen M.;Krajewski, Krzysztof;Baker, Richard W.;Miller, Victoria L.;Strahl, Brian D.

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We report a general method to examine the recognition of post-translational modifications (PTMs) by antibodies and proteins. We use this method to evaluate the binding of modification-specific antibodies and chromatin-associating factors to an array of high-purified, biotinylated peptides (derived from human histone sequences) harboring multiple PTMs printed onto streptavidin-coated glass slides. We find that modification-specific antibodies are both more promiscuous in their PTM recognition than expected and highly influenced by neighboring PTMs. Binding of chromatin-associating factors is also influenced by combinatorial PTMs, giving further support for the “Histone Code” hypothesis. Thus we report the first thorough characterization of PTM influence on antibody recognition and describe a tool for the rapid and inexpensive assessment of chromatin-associating factor binding specificity.
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