Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A cysteine protease from maize isolated in a complex with cystatin
Autore:
Yamada, T; Ohta, H; Shinohara, A; Iwamatsu, A; Shimada, H; Tsuchiya, T; Masuda, T; Takamiya, K;
Indirizzi:
Tokyo Inst Technol, Fac Biosci & Biotechnol, Dept Biol Sci, Midori Ku, Yokohama, Kanagawa 2268501, Japan Tokyo Inst Technol Yokohama Kanagawa Japan 2268501 anagawa 2268501, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan
Titolo Testata:
PLANT AND CELL PHYSIOLOGY
fascicolo: 2, volume: 41, anno: 2000,
pagine: 185 - 191
SICI:
0032-0781(200002)41:2<185:ACPFMI>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEINASE-INHIBITOR; MESOPHYLL PROTOPLASTS; MOLECULAR-CLONING; RICE SEEDS; PURIFICATION; EXPRESSION; CHLOROPLASTS; DEGRADATION; SENESCENCE; CDNA;
Keywords:
cystatin; cysteine protease (EC 3.4.22); maize; protease-inhibitor complex; SDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Yamada, T Tokyo Inst Technol, Fac Biosci & Biotechnol, Dept Biol Sci, Midori Ku, Yokohama, Kanagawa 2268501, Japan Tokyo Inst Technol Yokohama Kanagawa Japan 2268501 68501, Japan
Citazione:
T. Yamada et al., "A cysteine protease from maize isolated in a complex with cystatin", PLANT CEL P, 41(2), 2000, pp. 185-191

Abstract

We recently purified a latent but SDS-activated protease complex (40, 15- or 13-kDa proteins) from maize [Yamada et al. (1998) Plant Cell Physiol. 39: 106], Here, we revealed that the complex was composed of a cysteine protease (40 kDa) and a cystatin, cysteine protease inhibitor (15- or 13-kDa). This is the first report on the isolation of a complex consisting of a cystatin and a target cysteine protease from plants. Cloning of the cysteine protease revealed that it had low homology (25-30%) to other maize cysteine proteases cloned to date but was highly homologous to other plant cysteine proteases such as rice oryzain a (84%) and the homologs (50-80%). The cysteine protease expressed in Escherichia coil showed the same substrate and inhibitor specificities as the protease of the complex, demonstrating that the isolated cDNA clone exactly encodes the protease of the complex. The protease expressed in E. coli itself was active but not latent, probably because it was not bound to cystatin. It is most likely that in vitro activation ofthe protease complex by SDS is caused by the release of bound cystatin. The mRNA of protease was expressed in various tissues except for seeds.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 02:41:43