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

ABSTRACT: Increasing evidence suggests that histone posttranslational modifications (PTMs) function in a combinatorial fashion to regulate the diverse activities associated with chromatin. Yet how these patterns of histone PTMs influence the adapter proteins known to bind them is poorly understood. In addition, how histone-specific antibodies are influenced by these same patterns of PTMs is largely unknown. Here we examine the binding properties of histone-specific antibodies and histone-interacting proteins using peptide arrays containing a library of combinatorially modified histone peptides. We find that modification-specific antibodies are more promiscuous in their PTM recognition than expected and are highly influenced by neighboring PTMs. Furthermore, we find that the binding of histone-intera

SUBMITTER: Fuchs SM 

PROVIDER: S-EPMC3019281 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature