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Congruence between PM H+-ATPase and NADPH oxidase during root growth: a necessary probability
Abstract
Plasma membrane (PM) H+-ATPase and NADPH oxidase (NOX) are two key enzymes responsible for cell wall relaxation during elongation growth through apoplastic acidification and production of ˙OH radical via O 2˙-, respectively. Our experiments revealed a putative feed-forward loop between these enzymes in growing roots of Vigna radiata (L.) Wilczek seedlings. Thus, NOX activity was found to be dependent on proton gradient generated across PM by H+-ATPase as evident from pharmacological experiments using carbonyl cyanide m-chlorophenylhydrazone (CCCP; protonophore) and sodium ortho-vanadate (PM H+-ATPase inhibitor). Conversely, H+-ATPase activity retarded in response to different ROS scavengers [CuCl 2, N, N' -dimethylthiourea (DMTU) and catalase] and NOX inhibitors [ZnCl 2 and diphenyleneiodonium (DPI)], while H 2 O 2 promoted PM H+-ATPase activity at lower concentrations. Repressing effects of Ca+2 antagonists (La+3 and EGTA) on the activity of both the enzymes indicate its possible mediation. Since, unlike animal NOX, the plant versions do not possess proton channel activity, harmonized functioning of PM H+-ATPase and NOX appears to be justified. Plasma membrane NADPH oxidase and H+-ATPase are functionally synchronized and they work cooperatively to maintain the membrane electrical balance while mediating plant cell growth through wall relaxation.
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“A higher[Ca2+]cyt likely to have a feedback regulation on the activity of NADPH oxidase and also influences actin polymerization either directly by changing actin amino acids or indirectly by influencing the activities of actin-binding proteins (ABPs), which can result in actin polymerization or depolymerization”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Majumdar and Kar, 2018
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Metadata
- Authors
- Majumdar, A., & Kar, R. K.
- Affiliations
- Visva-Bharati University (IN)
- Corresponding author
- Kar, Rup Kumar
- Venue
- Protoplasma
- Published
- 2018-02-12
- Volume
- 255
- Issue
- 4
- Pages
- 1129-1137
- ISSN
- 0033-183X (ISSN-L)
- 1615-6102
- OpenAlex
- W2789128986
- Cited by
- 37
- References
- 58
- Citations by year
- 2025: 5 · 2024: 4 · 2023: 5 · 2022: 5 · 2021: 9 · 2020: 5 · 2019: 2 · 2018: 2
- FWCI
- 3.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- PROTOPLASMA (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University Grants Commission, New Delhi, India (F. No. 25-1/2014-15(BSR)/220/2009/(BSR))
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant nutrient uptake and metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- plasma membrane H+-ATPase, NADPH oxidase, root elongation, feed-forward loop, reactive oxygen species, hydrogen peroxide, calcium signaling, mungbean, diphenyleneiodonium, sodium orthovanadate
- MeSH terms
- Cell Membrane, Proton-Translocating ATPases, Plant Roots, NADPH Oxidases
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