ArticlePlant physiology2004
A novel role of water-soluble chlorophyll proteins in the transitory storage of chorophyllide.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 36 citations in OpenAlex.
- Effects of heat shock on photosynthesis-related characteristics and lipid profile of Cycas multipinnata and C. panzhihuaensis.BMC plant biology · 2022Article
- New homologues of Brassicaceae water-soluble chlorophyll proteins shed light on chlorophyll binding, spectral tuning, and molecular evolution.The FEBS journal · 2020Article
- Water in Oil Emulsions: A New System for Assembling Water-soluble Chlorophyll-binding Proteins with Hydrophobic Pigments.Journal of visualized experiments : JoVE · 2016Article
- Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Water-soluble chlorophyll protein (WSCP) of Arabidopsis is expressed in the gynoecium and developing silique.Planta · 2012Article
- A proteomic profiling approach to reveal a novel role of Brassica napus drought 22 kD/water-soluble chlorophyll-binding protein in young leaves during nitrogen remobilization induced by stressful conditions.Plant physiology · 2008Article
- The senescence-induced staygreen protein regulates chlorophyll degradation.The Plant cell · 2007Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All chlorophyll (Chl)-binding proteins involved in photosynthesis of higher plants are hydrophobic membrane proteins integrated into the thylakoids. However, a different category of Chl-binding proteins, the so-called water-soluble Chl proteins (WSCPs), was found in members of the Brassicaceae, Polygonaceae, Chenopodiaceae, and Amaranthaceae families. WSCPs from different plant species bind Chl a and Chl b in different ratios. Some members of the WSCP family are induced after drought and heat stress as well as leaf detachment. It has been proposed that this group of proteins might have a physiological function in the Chl degradation pathway. We demonstrate here that a protein that shared sequence homology to WSCPs accumulated in etiolated barley (Hordeum vulgare) seedlings exposed to light for 2 h. The novel 22-kD protein was attached to the outer envelope of barley etiochloroplasts, and import of the 27-kD precursor was light dependent and induced after feeding the isolated plastids the tetrapyrrole precursor 5-aminolevulinic acid. HPLC analyses and spectroscopic pigment measurements of acetone-extracted pigments showed that the 22-kD protein is complexed with chlorophyllide. We propose a novel role of WSCPs as pigment carriers operating during light-induced chloroplast development.
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