N-terminal acetylation: an essential protein modification emerges as an important regulator of stress responses. (26th June 2018)
- Record Type:
- Journal Article
- Title:
- N-terminal acetylation: an essential protein modification emerges as an important regulator of stress responses. (26th June 2018)
- Main Title:
- N-terminal acetylation: an essential protein modification emerges as an important regulator of stress responses
- Authors:
- Linster, Eric
Wirtz, Markus - Abstract:
- Abstract : In this review, we summarize the current knowledge on the NAT machinery in higher plants and discuss the potential function of NTA during biotic and abiotic stresses. Abstract: N-terminal acetylation (NTA) is a prevalent protein modification in eukaryotes. The majority of proteins are acetylated at their N-terminus in a co-translational manner by ribosome-associated N-terminal acetyltransferases (NATs). However, the recent discovery of Golgi membrane-localized NATs in metazoa, and plastid-localized NATs in plants challenged the dogma of static, co-translational imprinting of the proteome by NTA. Indeed, NTA by the cytosolic NatA is highly dynamic and under hormonal control in plants. Such active control has not been evidenced yet in other eukaryotes and might be an adaptation to the sessile lifestyle of plants forcing them to cope with diverse environmental challenges. The function of NTAs for individual proteins is distinct and yet unpredictable. In yeast and humans, NTA has been shown to affect protein–protein interactions, subcellular localization, folding, aggregation, or degradation of a handful of proteins. In particular, the impact of NTA on the protein turnover is documented by diverse examples in yeast. Consequently, NTA was recently dicovered to be a degradation signal in a distinct branch of the N-end rule pathway, ubiquitin-mediated proteolysis. In this review, we summarize the current knowledge on the NAT machinery in higher plants and discuss theAbstract : In this review, we summarize the current knowledge on the NAT machinery in higher plants and discuss the potential function of NTA during biotic and abiotic stresses. Abstract: N-terminal acetylation (NTA) is a prevalent protein modification in eukaryotes. The majority of proteins are acetylated at their N-terminus in a co-translational manner by ribosome-associated N-terminal acetyltransferases (NATs). However, the recent discovery of Golgi membrane-localized NATs in metazoa, and plastid-localized NATs in plants challenged the dogma of static, co-translational imprinting of the proteome by NTA. Indeed, NTA by the cytosolic NatA is highly dynamic and under hormonal control in plants. Such active control has not been evidenced yet in other eukaryotes and might be an adaptation to the sessile lifestyle of plants forcing them to cope with diverse environmental challenges. The function of NTAs for individual proteins is distinct and yet unpredictable. In yeast and humans, NTA has been shown to affect protein–protein interactions, subcellular localization, folding, aggregation, or degradation of a handful of proteins. In particular, the impact of NTA on the protein turnover is documented by diverse examples in yeast. Consequently, NTA was recently dicovered to be a degradation signal in a distinct branch of the N-end rule pathway, ubiquitin-mediated proteolysis. In this review, we summarize the current knowledge on the NAT machinery in higher plants and discuss the potential function of NTA during biotic and abiotic stresses. … (more)
- Is Part Of:
- Journal of experimental botany. Volume 69:Number 19(2018)
- Journal:
- Journal of experimental botany
- Issue:
- Volume 69:Number 19(2018)
- Issue Display:
- Volume 69, Issue 19 (2018)
- Year:
- 2018
- Volume:
- 69
- Issue:
- 19
- Issue Sort Value:
- 2018-0069-0019-0000
- Page Start:
- 4555
- Page End:
- 4568
- Publication Date:
- 2018-06-26
- Subjects:
- Co-translational modifications -- N-end rule pathway -- N-terminal acetylation -- protein degradation -- protein modifications -- protein translation -- ribosome
Botany -- Periodicals
Botany, Experimental -- Periodicals
Plant physiology -- Periodicals
580 - Journal URLs:
- http://ukcatalogue.oup.com/ ↗
http://jxb.oxfordjournals.org/ ↗ - DOI:
- 10.1093/jxb/ery241 ↗
- Languages:
- English
- ISSNs:
- 0022-0957
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4981.000000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12238.xml