Abstract:
:A type II ribosome-inactivating protein (RIP) was isolated from the bark tissue of Japanese elderberry (Sambucus sieboldiana) and named sieboldin-b. Sieboldin-b is a heterodimeric protein consisting of 27- and 33-kDa subunits and showed strong ribosome-inactivating activity in vitro but did not show in vivo toxicity. The amino acid sequence of sieboldin-b deduced from the structure of the cDNA showed that both subunits of sieboldin-b are encoded on a single precursor polypeptide. Sieboldin-b has a structure homologous with the Neu5Ac(alpha 2-6)Gal/GalNAc-specific bark lectin from S. sieboldiana (SSA) and also typical type II RIPs such as ricin and abrin. Detailed analyses of carbohydrate binding properties of sieboldin-b revealed that sieboldin-b binds to Gal/GalNAc, similar to ricin/abrin, in spite of its highly homologous structure with SSA. The biological properties of these toxins/lectins are compared, and the possible explanation for such diversity is discussed.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Rojo MA,Yato M,Ishii-Minami N,Minami E,Kaku H,Citores L,Girbés T,Shibuya Ndoi
10.1006/abbi.1997.9927subject
Has Abstractpub_date
1997-04-15 00:00:00pages
185-94issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(97)99927-6journal_volume
340pub_type
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