Journal article
Proteomic Insights into Trichome Responses to Elevated Elemental Stress in Cation Exchanger (CAX) Mutants
Plant and cell physiology, Vol.65(12), pp.1941-1957
21/12/2024
PMID: 39219543
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Abstract
Research on elemental distribution in plants is crucial for understanding nutrient uptake, environmental adaptation, and optimizing agricultural practices for sustainable food production. Plant trichomes, with their self-contained structures and easy accessibility, offer a robust model system for investigating elemental repartitioning. Transport proteins, such as the four functional cation exchangers (CAXs) in Arabidopsis, are low-affinity, high-capacity transporters primarily located on the vacuole. Mutants in these transporters have been partially characterized, with one of the phenotypes of the CAX1 mutant being altered tolerance to low-oxygen conditions. A simple visual screen demonstrated trichome density and morphology in cax1 and quadruple CAX (cax1-4: qKO) mutants remained unaltered. Here we used SXRF (Synchrotron X-Ray Fluorescence) to show that trichomes in CAX-deficient lines accumulated high levels of chlorine, potassium, calcium, and manganese. Proteomic analysis on isolated Arabidopsis trichomes. showed changes in protein abundance in response to changes in element accumulation. The CAX mutants showed an increased abundance of plasma membrane ATPase and vacuolar H-pumping proteins, and proteins associated with water movement and endocytosis, while also showing changes in proteins associated with the regulation of plasmodesmata. These findings advance our understanding of the integration of CAX transport with elemental homeostasis within trichomes and shed light on how plants modulate protein abundance under conditions of altered elemental levels.Research on elemental distribution in plants is crucial for understanding nutrient uptake, environmental adaptation, and optimizing agricultural practices for sustainable food production. Plant trichomes, with their self-contained structures and easy accessibility, offer a robust model system for investigating elemental repartitioning. Transport proteins, such as the four functional cation exchangers (CAXs) in Arabidopsis, are low-affinity, high-capacity transporters primarily located on the vacuole. Mutants in these transporters have been partially characterized, with one of the phenotypes of the CAX1 mutant being altered tolerance to low-oxygen conditions. A simple visual screen demonstrated trichome density and morphology in cax1 and quadruple CAX (cax1-4: qKO) mutants remained unaltered. Here we used SXRF (Synchrotron X-Ray Fluorescence) to show that trichomes in CAX-deficient lines accumulated high levels of chlorine, potassium, calcium, and manganese. Proteomic analysis on isolated Arabidopsis trichomes. showed changes in protein abundance in response to changes in element accumulation. The CAX mutants showed an increased abundance of plasma membrane ATPase and vacuolar H-pumping proteins, and proteins associated with water movement and endocytosis, while also showing changes in proteins associated with the regulation of plasmodesmata. These findings advance our understanding of the integration of CAX transport with elemental homeostasis within trichomes and shed light on how plants modulate protein abundance under conditions of altered elemental levels.
Details
- Title
- Proteomic Insights into Trichome Responses to Elevated Elemental Stress in Cation Exchanger (CAX) Mutants
- Creators
- Qi Guo - Southern Cross UniversityShayan Sarkar - Children's Nutrition Research Center at Baylor College of MedicineTracy Punshon - Dartmouth CollegeRyan Tappero - Brookhaven National LaboratoryBronwyn J Barkla - Southern Cross UniversityKendal D Hirschi - Children's Nutrition Research Center at Baylor College of Medicine
- Publication Details
- Plant and cell physiology, Vol.65(12), pp.1941-1957
- Publisher
- Oxford University Press; OXFORD
- Grant note
- DOE Office of Science by Brookhaven National Laboratory: DE-SC0012704 ARC LIEF project: LE170100192 National Science Foundation: 1557890 USDA: 3092-51000-061-00D National Institute of Health: R03 AI149201-02
This research used the XFM beamline (4-BM) of the NSLSII, a US Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Brookhaven National Laboratory under Contract No. DE-SC0012704, the mass spectrometry work was carried out on a SCIEX Triple TOF 6600 at IMB UQ funded through an ARC LIEF project LE170100192, the National Science Foundation (1557890 to T.P. and K.D.H.), USDA (3092-51000-061-00D to K.D.H.) and National Institute of Health (R03 AI149201-02).
- Identifiers
- 991013221213702368
- Copyright
- © The Author(s) 2024. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.
- Academic Unit
- Southern Cross Analytical Research Services; Faculty of Science and Engineering; Science
- Language
- English
- Resource Type
- Journal article