Dataset Information

Proteome imprinting by N-terminal acetylation is a vital hormone-regulated master switch during stress

ABSTRACT: N-terminal acetylation (NTA) catalyzed by N-terminal acetyltransferases (Nats) is among the most common protein modifications in eukaryotes, but its significance is still enigmatic. Characterization of the plant NatA complex reveals evolutionary conservation of NatA biochemical properties within higher eukaryotes and uncovers specific and essential functions of NatA for regulation of development, numerous biosynthetic pathways and stress responses in plants. We show that NTA decreases significantly in case of drought stress, since NatA abundance is rapidly down-regulated by the phytohormone abscisic acid. Accordingly, down-regulation of NatA by genetic engineering is sufficient for induction of the drought stress response and results in strikingly drought resistant plants. Thus, NTA by the NatA complex is a vital cellular surveillance mechanism during stress. We conclude that imprinting of the proteome by NatA is a master switch for control of metabolism, development and cellular stress responses and integrates stress signals by perceiving the hormone abscisic acid.

OTHER RELATED OMICS DATASETS IN: PRJNA273928

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Willy Bienvenut

LAB HEAD: Willy Bienvenut

PROVIDER: PXD002069 | Pride | 2016-06-14

REPOSITORIES: Pride

ACCESS DATA

Publications

Downregulation of N-terminal acetylation triggers ABA-mediated drought responses in Arabidopsis.

Linster Eric E Stephan Iwona I Bienvenut Willy V WV Maple-Grødem Jodi J Myklebust Line M LM Huber Monika M Reichelt Michael M Sticht Carsten C Møller Simon Geir SG Meinnel Thierry T Arnesen Thomas T Giglione Carmela C Hell Rüdiger R Wirtz Markus M

Nature communications 20150717

N-terminal acetylation (NTA) catalysed by N-terminal acetyltransferases (Nats) is among the most common protein modifications in eukaryotes, but its significance is still enigmatic. Here we characterize the plant NatA complex and reveal evolutionary conservation of NatA biochemical properties in higher eukaryotes and uncover specific and essential functions of NatA for development, biosynthetic pathways and stress responses in plants. We show that NTA decreases significantly after drought stress ...[more]

PMID: 26184543

Similar Datasets

Project description:In Arabidopsis thaliana the evolutionary conserved N-terminal acetyltransferase (Nat) complexes NatA and NatB co-translationally acetylate 60% of the proteome. Both have recently been implicated in the regulation of plant stress responses. While NatA mediates drought tolerance, NatB is required for pathogen resistance and the adaptation to high salinity and high osmolarity. Salt and osmotic stress impair protein folding and result in the accumulation of misfolded proteins in the endoplasmic reticulum (ER). The ER-membrane resident E3 ubiquitin ligase DOA10 targets misfolded proteins for degradation during ER stress and is conserved among eukaryotes. In yeast, DOA10 recognizes conditional degradation signals (Ac/N-degrons) created by NatA and NatB. Assuming that this mechanism is preserved in plants, the lack of Ac/N-degrons required for efficient removal of misfolded proteins might explain the sensitivity of NatB mutants to protein harming conditions. In this study, we investigate the response of NatB mutants to dithiothreitol (DTT) and tunicamycin (TM) induced ER stress. We report that NatB mutants are hypersensitive to DTT but not TM, suggesting that the DTT hypersensitivity is caused by an over-reduction of the cytosol rather than an accumulation of unfolded proteins in the ER. In line with this hypothesis, the cytosol of NatB depleted plants is constitutively over-reduced and a global transcriptome analysis reveals that their reductive stress response is permanently activated. Moreover, we demonstrate that doa10 mutants are susceptible to neither DTT nor TM, ruling out a substantial role of DOA10 in ER-associated protein degradation (ERAD) in plants. Contrary to previous findings in yeast, our data indicates that N-terminal acetylation (NTA) does not inhibit ER targeting of a substantial amount of proteins in plants. In summary, we provide further evidence that NatB-mediated imprinting of the proteome is vital for the response to protein-harming stress and rule out DOA10 as the sole recognin for substrates in the plant ERAD pathway.

Dataset Information

Proteome imprinting by N-terminal acetylation is a vital hormone-regulated master switch during stress

Publications

Downregulation of N-terminal acetylation triggers ABA-mediated drought responses in Arabidopsis.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure