Identification of a novel high‐affinity binding site for N‐acetylchitooligosaccharide elicitor in the membrane fraction from suspension‐cultured rice cells

FEBS Letters

Maliarik, Mary J.¹  Kuchitsu, Kazuyuki¹  Shibuya, Naoto¹  Kaku, Hanae¹ 

[1] Department of Cell Biology, National Institute of Agrobiological Resources, Tsukuba, Ibaraki, 305 Japan

关键词: N-Acetylchitooligosaccharide;    Elicitor;    Host-pathogen interaction;    Receptor;    Rice suspension culture;    PBS;    phosphate-buffered saline;    FAB-MS;    fast-atom-bombardment mass spectrometry;    DTT;    dithiothreitol;    EGTA;    ethyleneglycol-bis(β-aminoethyl ether)-N;    N;    N';    N'-tetraacetic acid;    HPLC;    high-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(93)80197-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Binding experiments using a ¹²⁵I-labeled tyramine conjugate of N-acetylchitooctaose, a highly potent elicitor for the induction of phytoalexin production in rice cells, and a microsomal membrane preparation from suspension-cultured rice cells showed the presence of a novel high-affinity binding site for this oligosaccharide. The binding of the ligand was saturable and the Scatchard plot analysis of the results indicated the presence of a single class of binding site with a K _d of 5.4 nM which is comparable with that reported for the binding of the hepta-β-glucoside elicitor in soybean membrane. The ligand binding was inhibited by unlabeled N-acetylchitoheptaose but not by its deacetylated form. These characteristics of this binding site coincide well with the specificity and sensitivity for the elicitor in several assay systems, suggesting the possible involvement of this binding site in the recognition of the elicitor in vivo.

【 授权许可】

Unknown