A Plant-Specific Protein Essential for Blue-Light-Induced Chloroplast Movements
Abstract
In Arabidopsis (Arabidopsis thaliana), light-dependent chloroplast movements are induced by blue light. When exposed to low fluence rates of light, chloroplasts accumulate in periclinal layers perpendicular to the direction of light, presumably to optimize light absorption by exposing more chloroplast area to the light. Under high light conditions, chloroplasts become positioned parallel to the incoming light in a response that can reduce exposure to light intensities that may damage the photosynthetic machinery. To identify components of the pathway downstream of the photoreceptors that mediate chloroplast movements (i.e. phototropins), we conducted a mutant screen that has led to the isolation of several Arabidopsis mutants displaying altered chloroplast movements. The plastid movement impaired1 (pmi1) mutant exhibits severely attenuated chloroplast movements under all tested fluence rates of light, suggesting that it is a necessary component for both the low- and high-light-dependant chloroplast movement responses. Analysis of pmi1 leaf cross sections revealed that regardless of the light condition, chloroplasts are more evenly distributed in leaf mesophyll cells than in the wild type. The pmi1-1 mutant was found to contain a single nonsense mutation within the open reading frame of At1g42550. This gene encodes a plant-specific protein of unknown function that appears to be conserved among angiosperms. Sequence analysis of the protein suggests that it may be involved in calcium-mediated signal transduction, possibly through protein–protein interactions.
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PMI1 is essential for chloroplast movement, and the pmi1 mutant exhibits substantially impaired chloroplast movement.
“PMI1, a C2 domain protein, is essential for chloroplast movement, and the pmi1 mutant exhibits substantially impaired chloroplast movement”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as DeBlasio et al., 2005
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References 73 · Cited by 102
- Authors
- DeBlasio, S. L., Luesse, D. L., & Hangarter, R. P.
- Affiliations
- Indiana University Bloomington (US)
- Department of Biology, Indiana University, Bloomington, Indiana 47405
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-08-19
- Volume
- 139
- Issue
- 1
- Pages
- 101-114
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- OpenAlex
- W2067647886
- Cited by
- 102
- References
- 73
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 7 · 2023: 6 · 2022: 3 · 2021: 3 · 2020: 3 · 2019: 1 · 2018: 5 · 2017: 2 · 2016: 8 · 2015: 4 · 2014: 2 · 2013: 6 · 2012: 6
- FWCI
- 7.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
- Locations
- PLANT PHYSIOLOGY (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- chloroplast movement, blue light, phototropin, Arabidopsis thaliana, calcium signaling, protein-protein interaction
- MeSH terms
- Actins, Amino Acid Sequence, Chloroplasts, Color, Cytoskeleton, Light, Molecular Sequence Data, Movement, Mutation, Signal Transduction, Sequence Alignment, Arabidopsis, Sequence Homology, Amino Acid, Gene Expression Regulation, Plant, Plant Leaves, Arabidopsis Proteins, Intracellular Signaling Peptides and Proteins
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