SPOTing Acetyl-Lysine Dependent Interactions
AbstractPost translational modifications have been recognized as chemical signals that create docking sites for evolutionary conserved effector modules, allowing for signal integration within large networks of interactions. Lysine acetylation in particular has attracted attention as a regulatory modification, affecting chromatin structure and linking to transcriptional activation. Advances in peptide array technologies have facilitated the study of acetyl-lysine-containing linear motifs interacting with the evolutionary conserved bromodomain module, which specifically recognizes and binds to acetylated sequences in histones and other proteins. Here we summarize recent work employing SPOT peptide technology to identify acetyl-lysine dependent interactions and document the protocols adapted in our lab, as well as our efforts to characterize such bromodomain-histone interactions. Our results highlight the versatility of SPOT methods and establish an affordable tool for rapid access to potential protein/modified-peptide interactions involving lysine acetylation. View Full-Text
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Picaud, S.; Filippakopoulos, P. SPOTing Acetyl-Lysine Dependent Interactions. Microarrays 2015, 4, 370-388.
Picaud S, Filippakopoulos P. SPOTing Acetyl-Lysine Dependent Interactions. Microarrays. 2015; 4(3):370-388.Chicago/Turabian Style
Picaud, Sarah; Filippakopoulos, Panagis. 2015. "SPOTing Acetyl-Lysine Dependent Interactions." Microarrays 4, no. 3: 370-388.