Isolation and partial characterization of a novel and uncommon two‐chain 64‐kDa ribosome‐inactivating protein from the bark of elder (Sambucus nigra L.)

FEBS Letters

Camafeita, Emilio¹  de Benito, Fernando M.²  Méndez, Enrique¹  Girbés, Tomás²  Citores, Lucı́a²  Iglesias, Rosario²  Ferreras, J.Miguel² 

[1] Centro Nacional de Biotecnologı́a, Consejo Superior de Investigaciones Cientı́ficas (CSIC), Canto Blanco, Madrid, Spain;Departamento de Bioquı́mica y Biologı́a Molecular, Facultad de Ciencias, Universidad de Valladolid, E-47005 Valladolid, Spain

关键词: Ribosome-inactivating proteins;    rRNA N-glycosidase;    Protein synthesis inhibition;    Basic nigrin b;    Nigrin b;    Sambucus nigra L.;    IC50;    concentration of inhibitory protein that gives 50% of inhibition in the rabbit reticulocyte lysate translation system;    Nigrin bb;    basic nigrin from bark;    PAGE;    polyacrylamide gel electrophoresis;    RIP(s);    ribosome-inactivating protein(s);    TMV;    Tobacco mosaic virus;   

DOI  :  10.1016/S0014-5793(97)00882-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel, strongly basic, two-chain ribosome-inactivating protein (RIP) with an apparent M _r of 64 000 by SDS-PAGE and 63469 by mass spectrometry analysis, that we have named basic nigrin b, has been found in the bark of elder (Sambucus nigra L.). The new protein does not agglutinate red blood cells, even at high concentrations and displays an unusually and extremely high activity towards animal ribosomes (IC₅₀ of 18 pg/ml for translation by rabbit reticulocyte lysates). However, it is inactive against plant and HeLa cells protein synthesis. Our functional and structural data are consistent with a heterodimeric structure for basic nigrin b of the type A-B*, B* being a truncated lectin lacking functional binding domains equivalent to the B (lectin) chain of the type 2 RIP SNA I and nigrin b present also in elder bark.

【 授权许可】

Unknown