Advanced methods for the analysis of chromatin-associated proteins.

Autor:	Guillen-Ahlers H; Department of Genetics, Texas Biomedical Research Institute, San Antonio, Texas; and., Shortreed MR; Department of Chemistry, University of Wisconsin, Madison, Wisconsin., Smith LM; Department of Chemistry, University of Wisconsin, Madison, Wisconsin., Olivier M; Department of Genetics, Texas Biomedical Research Institute, San Antonio, Texas; and molivier@txbiomedgenetics.org.
Jazyk:	angličtina
Zdroj:	Physiological genomics [Physiol Genomics] 2014 Jul 01; Vol. 46 (13), pp. 441-7. Date of Electronic Publication: 2014 May 06.
DOI:	10.1152/physiolgenomics.00041.2014
Abstrakt:	DNA-protein interactions are central to gene expression and chromatin regulation and have become one of the main focus areas of the ENCODE consortium. Advances in mass spectrometry and associated technologies have facilitated studies of these interactions, revealing many novel DNA-interacting proteins and histone posttranslational modifications. Proteins interacting at a single locus or at multiple loci have been targeted in these recent studies, each requiring a separate analytical strategy for isolation and analysis of DNA-protein interactions. The enrichment of target chromatin fractions occurs via a number of methods including immunoprecipitation, affinity purification, and hybridization, with the shared goal of using proteomics approaches as the final readout. The result of this is a number of exciting new tools, with distinct strengths and limitations that can enable highly robust and novel chromatin studies when applied appropriately. The present review compares and contrasts these methods to help the reader distinguish the advantages of each approach. (Copyright © 2014 the American Physiological Society.)
Databáze:	MEDLINE
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