Journal Article

Water-Soluble Chlorophyll Protein in Brassicaceae Plants is a Stress-Induced Chlorophyll-Binding Protein

Hiroyuki Satoh, Akira Uchida, Katsumi Nakayama and Mitsumasa Okada

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 42, issue 9, pages 906-911
Published in print September 2001 | ISSN: 0032-0781
Published online September 2001 | e-ISSN: 1471-9053 | DOI: https://dx.doi.org/10.1093/pcp/pce117
Water-Soluble Chlorophyll Protein in Brassicaceae Plants is a Stress-Induced Chlorophyll-Binding Protein

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  • Biochemistry
  • Molecular and Cell Biology
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Two kinds of water-soluble chlorophyll (Chl) proteins (WSCPs) have been found, e.g., a WSCP from Chenopodium, Atriplex, Polygonum, and Amaranthus species (class I) and that from Brassica, Raphanus, and Lepidium species (class II). Classes I and II WSCPs differ mainly in their photoconvertiblity. Class I WSCPs show a light-induced absorption change, whereas Class II WSCPs do not. The molecular and functional properties of Class I WSCP are largely uncertain. On the other hand, recent studies on the adaptation of plants to osmotic stress revealed the participation of drought-stress induced proteins with molecular masses of 20–22 kDa possessing a sequence similarity with class II WSCPs. This mini review focuses on the molecular signature of class II WSCPs. The physiological function of class II WSCPs has not been clarified either, but, their water-solubility, low Chl content, and stress-inducibility suggested little contribution to photosynthesis. Several molecular properties predicting its physiological role are as follows. The WSCP tetramer, may have only one or no Chl molecules in each subunit. All WSCPs possess a motif for Künitz-type proteinase inhibitor family in their sequence. WSCP is induced by drought- and heat-stresses suggesting its protective role during stress conditions. Monomeric recombinant apo-WSCP is able to remove Chls from the thylakoid membrane in aqueous solution and form into a tetramer. Brassica-WSCP contains a signal sequence targeted to endoplasmic reticulum. The highly conserved, C-terminal region is missing in the mature WSCP. Possible functions of class II WSCPs in plant tissues are discussed.

Keywords: Key words: Brassicaceae — Chlorophyll — Drought stress — Künitz proteinase inhibitor — Water-soluble Chl protein.; Abbreviations: Chlase, chlorophyllase; ER, endoplasmic reticulum; WSCP, water-soluble chlorophyll protein.

Journal Article.  4350 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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