ArticlePlant physiology2012
MES16, a member of the methylesterase protein family, specifically demethylates fluorescent chlorophyll catabolites during chlorophyll breakdown in Arabidopsis.
Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 96 citations in OpenAlex.
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- Unexpected Dual Function of Plant YUCCA Enzymes Links Chlorophyll Catabolism to Auxin Homeostasis.Angewandte Chemie (International ed. in English) · 2026Article
- Function and Evolution of the Plant MES Family of Methylesterases.Plants (Basel, Switzerland) · 2024Review
- The Effect of Ethephon on Ethylene and Chlorophyll inInternational journal of molecular sciences · 2024Article
- Side-chain modifications of phyllobilins may not be essential for chlorophyll degradation inPlant direct · 2022Article
- Transcriptomic Analysis Reveals LncRNAs Associated with Flowering ofCurrent issues in molecular biology · 2022Article
- Multiomics Approach To Decipher the Origin of Chlorophyll Content in Virgin Olive Oil.Journal of agricultural and food chemistry · 2022Article
- Evolution of chlorophyll degradation is associated with plant transition to land.The Plant journal : for cell and molecular biology · 2022Article
- Review
- Repressed OsMESL expression triggers reactive oxygen species-mediated broad-spectrum disease resistance in rice.Plant biotechnology journal · 2021Article
- An evergreen mind and a heart for the colors of fall.Journal of experimental botany · 2021Article
- Leaf senescence: progression, regulation, and application.Molecular horticulture · 2021Review
- Roles of stay-green (SGR) homologs during chlorophyll degradation in green plants.Botanical studies · 2020Review
- PheophorbidePlant physiology · 2020Article
- Cryptic chlorophyll breakdown in non-senescent green Arabidopsis thaliana leaves.Photosynthesis research · 2019Article
- The C-terminal cysteine-rich motif of NYE1/SGR1 is indispensable for its function in chlorophyll degradation in Arabidopsis.Plant molecular biology · 2019Article
- Fluctuating Light Interacts with Time of Day and Leaf Development Stage to Reprogram Gene Expression.Plant physiology · 2019Article
- Novel Types of Hypermodified Fluorescent Phyllobilins from Breakdown of Chlorophyll in Senescent Leaves of Grapevine (Vitis vinifera).Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Characterization of the pheophorbide a oxygenase/phyllobilin pathway of chlorophyll breakdown in grasses.Planta · 2018Article
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7 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
During leaf senescence, chlorophyll (Chl) is broken down to nonfluorescent chlorophyll catabolites (NCCs). These arise from intermediary fluorescent chlorophyll catabolites (FCCs) by an acid-catalyzed isomerization inside the vacuole. The chemical structures of NCCs from Arabidopsis (Arabidopsis thaliana) indicate the presence of an enzyme activity that demethylates the C13(2)-carboxymethyl group present at the isocyclic ring of Chl. Here, we identified this activity as methylesterase family member 16 (MES16; At4g16690). During senescence, mes16 leaves exhibited a strong ultraviolet-excitable fluorescence, which resulted from large amounts of different FCCs accumulating in the mutants. As confirmed by mass spectrometry, these FCCs had an intact carboxymethyl group, which slowed down their isomerization to respective NCCs. Like a homologous protein cloned from radish (Raphanus sativus) and named pheophorbidase, MES16 catalyzed the demethylation of pheophorbide, an early intermediate of Chl breakdown, in vitro, but MES16 also demethylated an FCC. To determine the in vivo substrate of MES16, we analyzed pheophorbide a oxygenase1 (pao1), which is deficient in pheophorbide catabolism and accumulates pheophorbide in the chloroplast, and a mes16pao1 double mutant. In the pao1 background, we additionally mistargeted MES16 to the chloroplast. Normally, MES16 localizes to the cytosol, as shown by analysis of a MES16-green fluorescent protein fusion. Analysis of the accumulating pigments in these lines revealed that pheophorbide is only accessible for demethylation when MES16 is targeted to the chloroplast. Together, these data demonstrate that MES16 is an integral component of Chl breakdown in Arabidopsis and specifically demethylates Chl catabolites at the level of FCCs in the cytosol.
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