NIH VideoCast - Mechanisms for regulating of histone ubiquitination and acetylation by the SAGA complex

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Mechanisms for regulating of histone ubiquitination and acetylation by the SAGA complex

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Air date:	Monday, November 16, 2015, 12:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 207 (20 Live, 187 On-demand)
Category:	Neuroscience
Runtime:	00:57:59
Description:	NIH Neuroscience Seminar Series Protein function is dynamically regulated in the cell by the attachment and subsequent removal of covalent post translational modifications. Acetylation and ubiquitination both occur in chromatin, the nucleoprotein complex into which eukaryotic DNA is packaged. Acetylation of the histoneproteins in chromatin is associated with activation of transcription, whereasubiquitination can be either an activating or a repressive mark, depending onwhich histone protein is modified. Ubiquitination of chromatin also plays arole in the response to DNA double-strand breaks, helping to recruit proteinsthat are required for DNA repair. Dr. Wolberger’s lab is interested in themolecular basis for these events, which ensure the integrity and expression ofthe genome. They use x-ray crystallography, enzymology, cell-based assays and avariety of biophysical tools to gain insights into the mechanisms underlying these essential cellular processes.

NLM Title:	Mechanisms for regulating of histone ubiquitination and acetylation by the SAGA complex / Cynthia Wolberger, Ph.D., Johns Hopkins University School of Medicine.
Author:	Wolberger, Cynthia. National Institutes of Health (U.S.),
Publisher:
Abstract:	(CIT): NIH Neuroscience Seminar SeriesProtein function is dynamically regulated in the cell by the attachment and subsequent removal of covalent post translational modifications. Acetylation and ubiquitination both occur in chromatin, the nucleoprotein complex into which eukaryotic DNA is packaged. Acetylation of the histoneproteins in chromatin is associated with activation of transcription, whereasubiquitination can be either an activating or a repressive mark, depending onwhich histone protein is modified. Ubiquitination of chromatin also plays arole in the response to DNA double-strand breaks, helping to recruit proteinsthat are required for DNA repair. Dr. Wolberger"s lab is interested in themolecular basis for these events, which ensure the integrity and expression of the genome. They use x-ray crystallography, enzymology, cell-based assays and avariety of biophysical tools to gain insights into the mechanisms underlying these essential cellular processes.
Subjects:	Acetylation Histones Transcription Factors Ubiquitination
Publication Types:	Lecture Webcast

NLM Classification:	QU 56
NLM ID:	101673103
CIT Live ID:	17417
Permanent link:	https://videocast.nih.gov/watch=17417

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