Differential up‐regulation by tRNAs of ribosome‐inactivating proteins

FEBS Letters

Pallanca, Alessandra¹  Brigotti, Maurizio¹  Sperti, Simonetta¹  Montanaro, Lucio¹  Carnicelli, Domenica¹  Alvergna, Paola¹ 

[1] Dipartimento di Patologia sperimentale dell'Università di Bologna, Via San Giacomo 14, I-40126 Bologna, Italy

关键词: Ribosome-inactivating protein;    Gelonin;    Agrostin;    Barley RIP;    PAP;    Tritin;    Luffin;    Trichokirin;    Trichosanthin;    tRNA;    PAP;    pokeweed antiviral protein;    RIP;    ribosome-inactivating protein;    S-100;    rat liver post-ribosomal supernatant;   

DOI  :  10.1016/0014-5793(95)01023-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Some plant ribosome-inactivating proteins (RIPs) with RNA-N-glycosidase activity on 28S RNA require, for the inactivation of ribosomes, the presence of macromolecular cofactors present in post-ribosomal supernatants. In the case of gelonin one of the cofactors is tRNA^Trp lacking one or two nucleotides at the 3′-CCA end [Brigotti, M., Carnicelli, D., Alvergna, P., Pallanca, A., Lorenzetti, R., Denaro, M., Sperti, S. and Montanaro, L. (1995) Biochem. J. 310, 249–253]. In the present study it is shown that tRNAs are involved in the up-regulation of all the cofactor-requiring RIPs up to now identified (agrostin, barley RIP, PAP and tritin, besides gelonin). Polyacrylamide gel electrophoresis shows that tRNA fractions with different mobilities stimulate different RIPs. With the identification of agrostin, the cofactor-requiring RIPs (italics) add to five out of a total of thirteen investigated: barley RIP, bryodin-R, gelonin, lychnin, momordin, momorcochin-S, PAP, saporin-6, tritin [Carnicelli, D., Brigotti, M., Montanaro, L. and Sperti, S. (1992) Biochem. Biophys. Res. Commun. 182, 579–582], agrostin, luffin, trichokirin and trichosanthin (present study).

【 授权许可】

Unknown