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α-Amanitin-resistant RNA polymerase II from carpophores of Amanita species accumulating amatoxins

1980; Elsevier BV; Volume: 607; Issue: 1 Linguagem: Inglês

10.1016/0005-2787(80)90224-5

1879-3002

Billy C. Johnson, James F. Preston,

Silymarin and Mushroom Poisoning

DNA-dependent RNA polymerase activities have been partially purified from carpophores of the amanitin (amatoxin)-accumulating species Amanita hygroscopica and Amanita suballiacea and the non-accumulating species Amanita brunnescens and Amanita alliacea. RNA polymerase II activities purified by ion-exchange chromatography were characterized with respect to ionic strength, template, and divalent metal ion requirements and sensitivities to inhibition by alpha-amanitin. The Ki values of alpha-amanitin for RNA polymerase II activities were: 2.0 . 10(-3) M for A. hygroscopica; 3.3 . 10(-3) M for A. suballiacea; 9.8 . 10(-6) M for A. brunnescens; 10.0 . 10(-6) M for A. alliacea. Further purification with DNA affinity chromatography of activities from A. suballiacea and A. brunnescens did not alter the apparent dissociation constants of alpha-amanitin from either enzyme. The correlation between amanitin sensitivity of RNA polymerase II and the quantity of amatoxins found in carpophores suggests these peptides may play a role in regulating transcription of messenger RNA during carpophore development.