Universität zu Köln

Hansen, Bogi Karbech, Gupta, Rajat, Baldus, Linda, Lyon, David ORCID: 0000-0001-5794-0456, Narita, Takeo ORCID: 0000-0002-2705-7838, Lammers, Michael ORCID: 0000-0003-4168-4640, Choudhary, Chunaram and Weinert, Brian T. (2019). Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation. Nat. Commun., 10. LONDON: NATURE PUBLISHING GROUP. ISSN 2041-1723

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Abstract

Lysine acetylation is a reversible posttranslational modification that occurs at thousands of sites on human proteins. However, the stoichiometry of acetylation remains poorly characterized, and is important for understanding acetylation-dependent mechanisms of protein regulation. Here we provide accurate, validated measurements of acetylation stoichiometry at 6829 sites on 2535 proteins in human cervical cancer (HeLa) cells. Most acetylation occurs at very low stoichiometry (median 0.02%), whereas high stoichiometry acetylation (>1%) occurs on nuclear proteins involved in gene transcription and on acetyltransferases. Analysis of acetylation copy numbers show that histones harbor the majority of acetylated lysine residues in human cells. Class I deacetylases target a greater proportion of high stoichiometry acetylation compared to SIRT1 and HDAC6. The acetyltransferases CBP and p300 catalyze a majority (65%) of high stoichiometry acetylation. This resource dataset provides valuable information for evaluating the impact of individual acetylation sites on protein function and for building accurate mechanistic models.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Hansen, Bogi Karbech UNSPECIFIED UNSPECIFIED UNSPECIFIED Gupta, Rajat UNSPECIFIED UNSPECIFIED UNSPECIFIED Baldus, Linda UNSPECIFIED UNSPECIFIED UNSPECIFIED Lyon, David UNSPECIFIED orcid.org/0000-0001-5794-0456 UNSPECIFIED Narita, Takeo UNSPECIFIED orcid.org/0000-0002-2705-7838 UNSPECIFIED Lammers, Michael UNSPECIFIED orcid.org/0000-0003-4168-4640 UNSPECIFIED Choudhary, Chunaram UNSPECIFIED UNSPECIFIED UNSPECIFIED Weinert, Brian T. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-154247
DOI:	10.1038/s41467-019-09024-0
Journal or Publication Title:	Nat. Commun.
Volume:	10
Date:	2019
Publisher:	NATURE PUBLISHING GROUP
Place of Publication:	LONDON
ISSN:	2041-1723
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language LYSINE ACETYLATION; COPY-NUMBER; QUANTIFICATION; SUCCINYLATION; ACETYLOME; ABUNDANCE; ACYLATION; REVEALS; IMPACT; SIRT3 Multiple languages Multidisciplinary Sciences Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/15424