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Titolo:
Water-soluble chlorophyll protein in Brassicaceae plants is a stress-induced chlorophyll-binding protein
Autore:
Satoh, H; Uchida, A; Nakayama, K; Okada, M;
Indirizzi:
Toho Univ, Dept Biomol Sci, Funabashi, Chiba 2748510, Japan Toho Univ Funabashi Chiba Japan 2748510 , Funabashi, Chiba 2748510, Japan
Titolo Testata:
PLANT AND CELL PHYSIOLOGY
fascicolo: 9, volume: 42, anno: 2001,
pagine: 906 - 911
SICI:
0032-0781(200109)42:9<906:WCPIBP>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
FUNCTIONAL EXPRESSION; MOLECULAR-CLONING; CHENOPODIUM-ALBUM; NAPUS LEAVES; GENE; SEQUENCE; DROUGHT; CAULIFLOWER; INHIBITOR; BREAKDOWN;
Keywords:
Brassicaceae; chlorophyll; drought stress; Kunitz proteinase inhibitor; water-soluble Chl protein;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Satoh, H Toho Univ, Dept Biomol Sci, Funabashi, Chiba 2748510, Japan Toho Univ Funabashi Chiba Japan 2748510 hi, Chiba 2748510, Japan
Citazione:
H. Satoh et al., "Water-soluble chlorophyll protein in Brassicaceae plants is a stress-induced chlorophyll-binding protein", PLANT CEL P, 42(9), 2001, pp. 906-911

Abstract

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 largelyuncertain. 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 Kunitz-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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 10:23:28