Publikation: Biochemical and Structural Consequences of NEDD8 Acetylation
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2024
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Deutsche Forschungsgemeinschaft (DFG): SFB 969, projects B03 and B09
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Core Facility der Universität Konstanz
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ChemBioChem. Wiley. 2024, 25(22), e202400478. ISSN 1439-4227. eISSN 1439-7633. Verfügbar unter: doi: 10.1002/cbic.202400478
Zusammenfassung
Similar to ubiquitin, the ubiquitin‐like protein NEDD8 is not only conjugated to other proteins but is itself subject to posttranslational modifications including lysine acetylation. Yet, compared to ubiquitin, only little is known about the biochemical and structural consequences of site‐specific NEDD8 acetylation. Here, we generated site‐specifically mono‐acetylated NEDD8 variants for each known acetylation site by genetic code expansion. We show that, in particular, acetylation of K11 has a negative impact on the usage of NEDD8 by the NEDD8‐conjugating enzymes UBE2M and UBE2F and that this is likely due to electrostatic and steric effects resulting in conformational changes of NEDD8. Finally, we provide evidence that p300 acts as a position‐specific NEDD8 acetyltransferase.
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570 Biowissenschaften, Biologie
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KIENLE, Simon Maria, Tobias SCHNEIDER, Christine BERNECKER, Janina BRACKER, Andreas MARX, Michael KOVERMANN, Martin SCHEFFNER, Katrin STUBER, 2024. Biochemical and Structural Consequences of NEDD8 Acetylation. In: ChemBioChem. Wiley. 2024, 25(22), e202400478. ISSN 1439-4227. eISSN 1439-7633. Verfügbar unter: doi: 10.1002/cbic.202400478BibTex
@article{Kienle2024-11-18Bioch-70448,
title={Biochemical and Structural Consequences of NEDD8 Acetylation},
year={2024},
doi={10.1002/cbic.202400478},
number={22},
volume={25},
issn={1439-4227},
journal={ChemBioChem},
author={Kienle, Simon Maria and Schneider, Tobias and Bernecker, Christine and Bracker, Janina and Marx, Andreas and Kovermann, Michael and Scheffner, Martin and Stuber, Katrin},
note={Article Number: e202400478}
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<dcterms:abstract>Similar to ubiquitin, the ubiquitin‐like protein NEDD8 is not only conjugated to other proteins but is itself subject to posttranslational modifications including lysine acetylation. Yet, compared to ubiquitin, only little is known about the biochemical and structural consequences of site‐specific NEDD8 acetylation. Here, we generated site‐specifically mono‐acetylated NEDD8 variants for each known acetylation site by genetic code expansion. We show that, in particular, acetylation of K11 has a negative impact on the usage of NEDD8 by the NEDD8‐conjugating enzymes UBE2M and UBE2F and that this is likely due to electrostatic and steric effects resulting in conformational changes of NEDD8. Finally, we provide evidence that p300 acts as a position‐specific NEDD8 acetyltransferase.</dcterms:abstract>
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