N-terminomics reveals control of Arabidopsis seed storage proteins and proteases by the Arg/N-end rule pathway

Bibliographische Detailangaben
Veröffentlicht in:	The New phytologist. - 1979. - 218(2018), 3 vom: 01. Mai, Seite 1106-1126
1. Verfasser:	Zhang, Hongtao (VerfasserIn)
Weitere Verfasser:	Gannon, Lucy, Hassall, Kirsty L, Deery, Michael J, Gibbs, Daniel J, Holdsworth, Michael J, van der Hoorn, Renier A L, Lilley, Kathryn S, Theodoulou, Frederica L
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2018
Zugriff auf das übergeordnete Werk:	The New phytologist
Schlagworte:	Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana TAILS N-end rule N-terminomics cruciferin protease quantitative proteomics tandem mass tag (TMT) mehr... Arabidopsis Proteins Peptides RNA, Messenger Seed Storage Proteins Arginine 94ZLA3W45F Endopeptidases EC 3.4.-

Beschreibung
Zusammenfassung:	© 2017 The Authors. New Phytologist © 2017 New Phytologist Trust. The N-end rule pathway of targeted protein degradation is an important regulator of diverse processes in plants but detailed knowledge regarding its influence on the proteome is lacking. To investigate the impact of the Arg/N-end rule pathway on the proteome of etiolated seedlings, we used terminal amine isotopic labelling of substrates with tandem mass tags (TMT-TAILS) for relative quantification of N-terminal peptides in prt6, an Arabidopsis thaliana N-end rule mutant lacking the E3 ligase PROTEOLYSIS6 (PRT6). TMT-TAILS identified over 4000 unique N-terminal peptides representing c. 2000 protein groups. Forty-five protein groups exhibited significantly increased N-terminal peptide abundance in prt6 seedlings, including cruciferins, major seed storage proteins, which were regulated by Group VII Ethylene Response Factor (ERFVII) transcription factors, known substrates of PRT6. Mobilisation of endosperm α-cruciferin was delayed in prt6 seedlings. N-termini of several proteases were downregulated in prt6, including RD21A. RD21A transcript, protein and activity levels were downregulated in a largely ERFVII-dependent manner. By contrast, cathepsin B3 protein and activity were upregulated by ERFVIIs independent of transcript. We propose that the PRT6 branch of the pathway regulates protease activities in a complex manner and optimises storage reserve mobilisation in the transition from seed to seedling via control of ERFVII action
Beschreibung:	Date Completed 01.10.2019 Date Revised 14.03.2024 published: Print-Electronic CommentIn: New Phytol. 2018 May;218(3):879-881. - PMID 29658638 Citation Status MEDLINE
ISSN:	1469-8137
DOI:	10.1111/nph.14909