Proteomics

Dataset Information

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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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Dataset's files

Source:
Action DRS
DiUb_K11_K48Ac_results.zip Other
Q2106_SMK_PRM_DiUb_-AcCoA_1_047.raw Raw
Q2106_SMK_PRM_DiUb_-AcCoA_2_048.raw Raw
Q2106_SMK_PRM_DiUb_-AcCoA_3_049.raw Raw
Q2106_SMK_PRM_DiUb_-p300_1_052.raw Raw
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Publications

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]

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