Abstract
Copyright: © 2013 Tackett AJ. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Mass spectrometry has played a vital role in defining what we understand about mechanisms regulating chromatin structure and function. With the speed, sensitivity and resolution of new generation mass spectrometers, researchers are now well-positioned to not only analyze bulk chromatin features, but to also begin to explore lower abundance chromatin signatures that help define the detailed epigenetic landscape of a chromosome. The components of chromatin that have been the primary focus of analysis by mass spectrometry are proteins and protein posttranslational modifications (PTMs). Below I discuss each of these components and provide insight into how mass spectrometry is helping to reshape how we study epigenetic mechanisms.
Highlights
Mass spectrometry has played a vital role in defining what we understand about mechanisms regulating chromatin structure and function
There are a variety of proteins and protein complexes that make up chromatin
As detailed above for a histone acetyltransferase, proteins can be directed to particular regions of chromatin to drive various activities
Summary
Mass spectrometry has played a vital role in defining what we understand about mechanisms regulating chromatin structure and function. There are a variety of proteins and protein complexes that make up chromatin. As detailed above for a histone acetyltransferase, proteins can be directed to particular regions of chromatin to drive various activities.
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