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Chasing Tails: Cathepsin-L Improves Structural Analysis of Histones by HX-MS.


ABSTRACT: The N-terminal regions (tails) of histone proteins are dynamic elements that protrude from the nucleosome and are involved in many aspects of chromatin organization. Their epigenetic role is well-established, and post-translational modifications present on these regions contribute to transcriptional regulation. Considering their biological significance, relatively few structural details have been established for histone tails, mainly because of their inherently disordered nature. Although hydrogen/deuterium exchange mass spectrometry (HX-MS) is well-suited for the analysis of dynamic structures, it has seldom been employed in this context, presumably because of the poor N-terminal coverage provided by pepsin. Inspired from histone-clipping events, we profiled the activity of cathepsin-L un

SUBMITTER: Papanastasiou M 

PROVIDER: S-EPMC6773551 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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