From start to finish: amino-terminal protein modifications as degredation signals in plant

Gibbs, Daniel J. and Bailey, Mark and Tedds, Hannah M. and Holdsworth, Michael J. (2016) From start to finish: amino-terminal protein modifications as degredation signals in plant. New Phytologist, 211 (4). pp. 1188-1194. ISSN 1469-8137

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Abstract

The amino- (N-) terminus (Nt) of a protein can undergo a diverse array of co- and posttranslational modifications. Many of these create degradation signals (N-degrons) that mediate protein destruction via the N-end rule pathway of ubiquitin-mediated proteolysis. In plants, the N-end rule pathway has emerged as a major system for regulated control of protein stability. Nt-arginylation-dependent degradation regulates multiple growth, development and stress responses, and recently identified functions of Nt-acetylation can also be linked to effects on the in vivo half-lives of Nt-acetylated proteins. There is also increasing evidence that N- termini could act as important protein stability determinants in plastids. Here we review recent advances in our understanding of the relationship between the nature of protein N-termini, Nt- processing events and proteolysis in plants.

Item Type: Article
Additional Information: This is the peer reviewed version of the following article: Gibbs, D. J., Bailey, M., Tedds, H. M. and Holdsworth, M. J. (2016), From start to finish: amino-terminal protein modifications as degradation signals in plants. New Phytologist, 211: 1188–1194. doi: 10.1111/nph.14105, which has been published in final form at http://onlinelibrary.wiley.com/wol1/doi/10.1111/nph.14105/abstract. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
Keywords: N-degron, N-end rule, Nt-acetylation, N-terminus, Protease, Protein modification, Proteolysis, Ubiquitin, Proteasome system
Schools/Departments: University of Nottingham, UK > Faculty of Science > School of Biosciences > Division of Plant and Crop Sciences
Identification Number: https://doi.org/10.1111/nph.14105
Depositing User: Dakin, Doreen
Date Deposited: 13 Sep 2016 13:29
Last Modified: 29 Nov 2016 01:08
URI: http://eprints.nottingham.ac.uk/id/eprint/36283

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