| Literature DB >> 19751687 |
Liyun Lin1, Qiang Fu, Berea A R Williams, Abdelhamid M Azzaz, Michael A Shogren-Knaak, John C Chaput, Stuart Lindsay.
Abstract
Histone acetylation plays an important role in the regulation of gene expression. A DNA aptamer generated by in vitro selection to be highly specific for histone H4 protein acetylated at lysine 16 was used as a recognition element for atomic force microscopy-based recognition imaging of synthetic nucleosomal arrays with precisely controlled acetylation. The aptamer proved to be reasonably specific at recognizing acetylated histones, with recognition efficiencies of 60% on-target and 12% off-target. Though this selectivity is much poorer than the >2000:1 equilibrium specificity of the aptamer, it is a large improvement on the performance of a ChIP-quality antibody, which is not selective at all in this application, and it should permit high-fidelity recognition with repeated imaging. The ability to image the precise location of posttranslational modifications may permit nanometer-scale investigation of their effect on chromatin structure.Entities:
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Year: 2009 PMID: 19751687 PMCID: PMC2749789 DOI: 10.1016/j.bpj.2009.06.045
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033