ArticlePlant physiology2014
Proteins with high turnover rate in barley leaves estimated by proteome analysis combined with in planta isotope labeling.
Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 140 citations in OpenAlex.
- Protein turnover in plants-cost of synthesis, repair, and crop engineering opportunities.Plant physiology · 2026Review
- Metabolic flux analysis in leaf metabolism quantifies the link between photorespiration and one carbon metabolism.Nature plants · 2025Article
- Comparative proteomic analysis of desiccation responses in recalcitrant Quercus acutissima seeds.Plant molecular biology · 2025Article
- Remodelled ribosomal populations synthesize a specific proteome in proliferating plant tissue during cold.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Adaptive responses of plants to light stress: mechanisms of photoprotection and acclimation. A review.Frontiers in plant science · 2025Review
- EARLY NODULIN93 acts via cytochrome c oxidase to alter respiratory ATP production and root growth in plants.The Plant cell · 2024Article
- CO-EXPRESSED WITH PSI ASSEMBLY1 (CEPA1) is a photosystem I assembly factor in Arabidopsis.The Plant cell · 2024Article
- Structure, function, and assembly of PSI in thylakoid membranes of vascular plants.The Plant cell · 2024Review
- Elevated Temperature Effects on Protein Turnover Dynamics inInternational journal of molecular sciences · 2024Article
- Methyl viologen-induced changes in the Arabidopsis proteome implicate PATELLIN 4 in oxidative stress responses.Journal of experimental botany · 2024Article
- Changing turn-over rates regulate abundance of tryptophan, GS biosynthesis, IAA transport and photosynthesis proteins in Arabidopsis growth defense transitions.BMC biology · 2023Article
- Seven plant capacities to adapt to abiotic stress.Journal of experimental botany · 2023Review
- The Relevance of Time in Biological Scaling.Biology · 2023Review
- Molecular dynamics of seed priming at the crossroads between basic and applied research.Plant cell reports · 2023Review
- Evaluation of GC/MS-BasedMetabolites · 2023Article
- Research progress on maintaining chloroplast homeostasis under stress conditions: a review.Acta biochimica et biophysica Sinica · 2023Review
- Tuning photosynthetic oxygen for hydrogen evolution in synergistically integrated, sulfur deprived consortia of Coccomyxa chodatii and Rhodobium gokarnense at dim and high light.Photosynthesis research · 2023Article
- The lifetime of the oxygen-evolving complex subunit PSBO depends on light intensity and carbon availability in Chlamydomonas.Plant, cell & environment · 2023Article
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- Photosystems under high light stress: throwing light on mechanism and adaptation.Photosynthetica · 2023Review
1 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein turnover is a key component in cellular homeostasis; however, there is little quantitative information on degradation kinetics for individual plant proteins. We have used (15)N labeling of barley (Hordeum vulgare) plants and gas chromatography-mass spectrometry analysis of free amino acids and liquid chromatography-mass spectrometry analysis of proteins to track the enrichment of (15)N into the amino acid pools in barley leaves and then into tryptic peptides derived from newly synthesized proteins. Using information on the rate of growth of barley leaves combined with the rate of degradation of (14)N-labeled proteins, we calculate the turnover rates of 508 different proteins in barley and show that they vary by more than 100-fold. There was approximately a 9-h lag from label application until (15)N incorporation could be reliably quantified in extracted peptides. Using this information and assuming constant translation rates for proteins during the time course, we were able to quantify degradation rates for several proteins that exhibit half-lives on the order of hours. Our workflow, involving a stringent series of mass spectrometry filtering steps, demonstrates that (15)N labeling can be used for large-scale liquid chromatography-mass spectrometry studies of protein turnover in plants. We identify a series of abundant proteins in photosynthesis, photorespiration, and specific subunits of chlorophyll biosynthesis that turn over significantly more rapidly than the average protein involved in these processes. We also highlight a series of proteins that turn over as rapidly as the well-known D1 subunit of photosystem II. While these proteins need further verification for rapid degradation in vivo, they cluster in chlorophyll and thiamine biosynthesis.
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