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Titolo:
Binding site for chitin oligosaccharides in the soybean plasma membrane
Autore:
Day, RB; Okada, M; Ito, Y; Tsukada, K; Zaghouani, H; Shibuya, N; Stacey, G;
Indirizzi:
Univ Tennessee, Dept Microbiol, Knoxville, TN 37996 USA Univ Tennessee Knoxville TN USA 37996 Microbiol, Knoxville, TN 37996 USA Univ Tennessee, Ctr Legume Res, Knoxville, TN 37996 USA Univ Tennessee Knoxville TN USA 37996 Legume Res, Knoxville, TN 37996 USA Natl Inst Agrobiol Resources, Dept Glycobiol, Tsukuba, Ibaraki 305, Japan Natl Inst Agrobiol Resources Tsukuba Ibaraki Japan 305 Ibaraki 305, Japan
Titolo Testata:
PLANT PHYSIOLOGY
fascicolo: 3, volume: 126, anno: 2001,
pagine: 1162 - 1173
SICI:
0032-0889(200107)126:3<1162:BSFCOI>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIGH-AFFINITY BINDING; CULTURED RICE CELLS; N-ACETYLCHITOOLIGOSACCHARIDE ELICITOR; BRADYRHIZOBIUM-JAPONICUM; EARLY NODULIN; NOD FACTORS; STRUCTURAL REQUIREMENTS; PHYTOALEXIN PRODUCTION; NODULATION SIGNALS; BIOTIC ELICITOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Stacey, G Univ Tennessee, Dept Microbiol, M409 Walters Life Sci Bldg, Knoxville, TN 37996 USA Univ Tennessee M409 Walters Life Sci Bldg Knoxville TN USA 37996
Citazione:
R.B. Day et al., "Binding site for chitin oligosaccharides in the soybean plasma membrane", PLANT PHYSL, 126(3), 2001, pp. 1162-1173

Abstract

Affinity cross-linking of the plasma membrane fraction to an I-125-labeledchitin oligosaccharide led to the identification and characterization of an 85-kD, chitin binding protein in plasma membrane-enriched fractions from both suspension-cultured soybean cells and root tissue, inhibition analysisindicated a binding preference for larger (i.e. degrees of polymerization = 8) N-acetylated chitin molecules with a 50% inhibition of initial activity value of approximately 50 nM. N-Acetyl-glucosamine and chitobiose showed no inhibitory effects at concentrations as high as 250 muM. it is noteworthy that the major lipo-chitin oligosaccharide Nod signal produced by Bradyrhizobium japonicum was also shown to be a competitive inhibitor of ligand binding. However, the binding site appeared to recognize the chitin portion of the Nod signal, and it is unlikely that this binding activity, representsa specific Nod signal receptor. Chitooligosaccharide specificity for induction of medium alkalinization and the generation of reactive oxygen in suspension-cultured cells paralleled the binding activity. Taken together, the presence of the chitin binding protein in the plasma membrane fraction and the specificity and induction of a biological response upon ligand binding suggest a role for the protein as an initial response mechanism for chitin perception in soybean (Glycine max).

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Documento generato il 26/09/20 alle ore 13:50:52