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Protein abundance changes in response to high light treatment

ABSTRACT: To characterize Arabidopsis proteomics and transcritomics changes in response to high light treatment. We quantify specific transcipts and protein abundance changes under both control and high light stress conditions. We aim to investigate the causality and interconnection of transcription and protein abundance change by an in-depth analysis of protein turnover, RNA-seq and 15N spike-in quantitative proteomics.

INSTRUMENT(S): LTQ Orbitrap

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

TISSUE(S): Shoot

SUBMITTER: Lei Li

LAB HEAD: Harvey Millar

PROVIDER: PXD010888 | Pride | 2022-07-12

REPOSITORIES: Pride

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			Action	DRS
	F1_1.dat	Other
	F1_1.raw	Raw
	F1_10.dat	Other
	F1_10.raw	Raw
	F1_11.dat	Other

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Publications

Enzymes degraded under high light maintain proteostasis by transcriptional regulation in <i>Arabidopsis</i>.

Li Lei L Duncan Owen O Ganguly Diep R DR Lee Chun Pong CP Crisp Peter A PA Wijerathna-Yapa Akila A Salih Karzan K Trösch Josua J Pogson Barry J BJ Millar A Harvey AH

Proceedings of the National Academy of Sciences of the United States of America 20220512 20

Photoinhibitory high light stress in Arabidopsis leads to increases in markers of protein degradation and transcriptional up-regulation of proteases and proteolytic machinery, but proteostasis is largely maintained. We find significant increases in the in vivo degradation rate for specific molecular chaperones, nitrate reductase, glyceraldehyde-3 phosphate dehydrogenase, and phosphoglycerate kinase and other plastid, mitochondrial, peroxisomal, and cytosolic enzymes involved in redox shuttles. C ...[more]

PMID: 35549553

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Protein turnover rates under high light treatment

Project description:To characterize Arabidopsis proteomics and transcritomics changes in response to high light treatment. We quantify specific transcipts and protein abundance changes under both control and high light stress conditions. We aim to investigate the causality and interconnection of transcription and protein abundance change by an in-depth analysis of protein turnover, RNA-seq and 15N spike-in quantitative proteomics.

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Arabidopsis, protein turnover, plastid, leaf growth and development-15N progressive labelling

Project description:In order to characterize plant protein degradation rates and understand their determinants as they relate to plant growth rate, we have applied 15N labelling approaches in leaves of the Arabidopsis rosette. We found a series of leaves in Arabidopsis plants for which the proteome was stable over time and degradation rates of individual proteins could thus be measured by considering the dilution of total protein abundance through growth. By progressively labelling new peptides with 15N and measuring the decrease in the abundance of over 60,000 peptides with natural isotope abundance profiles we determined the degradation rate of 1228 proteins. The exponential constant of the decay rate (KD) for each protein calculated from the relative isotope abundance of each peptide and the fold change in protein abundance during growth showed a wide distribution, ranging from 0 to 2 per day. This showed Arabidopsis protein half-lives vary from several hours to several months. In assessing intrinsic factors to explain these protein degradation rates, little effect of the N-end amino acid of proteins or of protein aggregation propensity were found, however protein complex membership and specific protein domains were strong predictors of degradation rate. We found new rapidly degrading subunits in a variety of protein complexes in plastids, identified the set of plant proteins whose degradation rate changes in different leaves of the rosette and correlated with leaf growth rate, and calculated the protein turnover energy costs in different leaves and their key determinants within the proteome.

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Arabidopsis, protein turnover, plastid, leaf growth and development-15N fully labelling as reference

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