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Mapping degradation signals and pathways in a eukaryotic N-terminome

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Summary: Most eukaryotic proteins are N-terminally acetylated. This modification can be recognized as a signal for selective protein degradation (degron) by the N-end rule pathways. However, the prevalence and specificity of such degrons in the proteome are unclear. Here, by systematically examining...

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Main Authors: Kats, Ilia (Author) , Khmelinskii, Anton (Author) , Kschonsak, Marc (Author) , Huber, Florian (Author) , Knieß, Robert A. (Author) , Bartosik, Anna (Author) , Knop, Michael (Author)
Format: Article (Journal)
Language:English
Published: May 3, 2018
In: Molecular cell
Year: 2018, Volume: 70, Issue: 3, Pages: 488-501.e5
ISSN:1097-4164
DOI:10.1016/j.molcel.2018.03.033
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Author Notes:authors Ilia Kats, Anton Khmelinskii, Marc Kschonsak, Florian Huber, Robert A. Knieß, Anna Bartosik, Michael Knop
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Summary:Summary: Most eukaryotic proteins are N-terminally acetylated. This modification can be recognized as a signal for selective protein degradation (degron) by the N-end rule pathways. However, the prevalence and specificity of such degrons in the proteome are unclear. Here, by systematically examining how protein turnover is affected by N-terminal sequences, we perform a comprehensive survey of degrons in the yeast N-terminome. We find that approximately 26% of nascent protein N termini encode cryptic degrons. These degrons exhibit high hydrophobicity and are frequently recognized by the E3 ubiquitin ligase Doa10, suggesting a role in protein quality control. In contrast, N-terminal acetylation rarely functions as a degron. Surprisingly, we identify two pathways where N-terminal acetylation has the opposite function and blocks protein degradation through the E3 ubiquitin ligase Ubr1. Our analysis highlights the complexity of N-terminal degrons and argues that hydrophobicity, not N-terminal acetylation, is the predominant feature of N-terminal degrons in nascent proteins.
Item Description:Gesehen am 24.05.2017
Physical Description:Online Resource
ISSN:1097-4164
DOI:10.1016/j.molcel.2018.03.033

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