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P300 acetylates Ub and linear Ub dimers

ABSTRACT: In this project we present the identification of in vitro acetylation of Ub by the acetyltransferase p300. Free monomeric Ub or M1-linked linear Ub dimers (diUb) were incubated in vitro with p300 in presence or absence of acetyl-Coenzyme A (AcCoA). For identification of the acetylation status of the respective Ub variants parallel reaction monitoring (PRM), a targeted-MS approach, was used.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Simon Kienle

LAB HEAD: Prof. Dr. Martin Scheffner

PROVIDER: PXD028813 | Pride | 2022-10-14

REPOSITORIES: Pride

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Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function.

Kienle Simon Maria SM Schneider Tobias T Stuber Katrin K Globisch Christoph C Jansen Jasmin J Stengel Florian F Peter Christine C Marx Andreas A Kovermann Michael M Scheffner Martin M

Nature communications 20220916 1

Covalent attachment of ubiquitin (Ub) to proteins is a highly versatile posttranslational modification. Moreover, Ub is not only a modifier but itself is modified by phosphorylation and lysine acetylation. However, the functional consequences of Ub acetylation are poorly understood. By generation and comprehensive characterization of all seven possible mono-acetylated Ub variants, we show that each acetylation site has a particular impact on Ub structure. This is reflected in selective usage of ...[more]

PMID: 36114200

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