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Molecular action of tricholin, a ribosome‐inactivating protein isolated from Trichoderma viride
Author(s) -
Lin A.,
Chen C.K.,
Chen Y.J.
Publication year - 1991
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1991.tb01860.x
Subject(s) - ribosome , reticulocyte , biology , lysis , ribosome inactivating protein , trichoderma viride , protein biosynthesis , ribosomal rna , biochemistry , rna , molecular mass , cleavage (geology) , enzyme , botany , paleontology , fracture (geology) , gene
Summary 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 × 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 α‐sarcin RNA fragment, from reticulocyte ribosomal RNA. This reaction to ribosomes mimics that of α‐sarcin. The antibody of α‐sarcin strongly cross‐reacts with tricholin, while the antibody of tricholin shows a weak reaction with α‐sarcin.