Molecular action of tricholin, a ribosome-inactivating protein isolated from Trichoderma viride.
An extracellular protein was isolated from a species of soil-borne fungi (Trichoderma viride) and its amino acid composition has been determined. The protein is acidic with a molecular mass of 14,200 daltons and is given the trivial name tricholin. Tricholin is a potent inhibitor of cell-free protein synthesis. When rabbit reticulocyte lysate was incubated with tricholin at a concentration of 6.3 x 10(-7) M, it completely abolished the capacity of the lysate to support protein synthesis. The inhibition appears to be due to its reaction to ribosomes, since it generates a specific cleavage product, an alpha-sarcin RNA fragment, from reticulocyte ribosomal RNA. This reaction to ribosomes mimics that of alpha-sarcin. The antibody of alpha-sarcin strongly cross-reacts with tricholin, while the antibody of tricholin shows a weak reaction with alpha-sarcin.
Lin
A
A
Institute of Genetics, National Yang-Ming Medical College, Taipei, Taiwan, Republic of China.
Chen
C K
CK
Chen
Y J
YJ
D002474:Cell-Free System / Q000187:drug effects; D005656:Fungal Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D012338:RNA, Ribosomal, 23S / Q000187:drug effects / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*; D014242:Trichoderma / Q000737:chemistry*
D005656:Fungal Proteins; D011500:Protein Synthesis Inhibitors; D012338:RNA, Ribosomal, 23S