Light-induced Activation of Cytoplasmic Protein Synthesis in Verticillium agaricinum
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Abstract The level of protein synthetic activity in dark‐grown cultures of Verticillium agaricinum was significantly enhanced by light. As expected the enhancement of protein synthetic activity was accompanied by a transformation of cytoplasmic monoribosomes to polyribosomes. Amino acid incorporation studies utilizing the synthetic mRNA, poly (U), suggest that the transformation was preceded by an activation of pre‐existing ribosomes. The change in ribosome activity related, at least in part, to an increase in the level of peptidyl‐tRNA associated with the ribosomes. In this regard the response of V. agaricinum ribosomes was similar to ribosome activation in several higher plant systems. The initial response at the level of the ribosome remains to be elucidated.Keywords:
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Abstract Isolation of ribosomes and assay systems for testing the translational apparatus have been part of the experimental routine of many laboratories for more than two decades, and excellent collections of the methods have been published previously, including two books in this series. However, a number of methods have been gradually and continuously improved and optimized. Major developments have included the improvement of ribosome isolation procedures, the establishment of highly efficient assay systems, and the application of heteropolymeric mRNA. The protocols in this chapter are concerned with the isolation of polysomes, ribosomes, and ribosomal subunits from prokaryotic and eukaryotic sources, as well as test systems for both total protein synthesis and single ribosomal functions, taking into account the recent developments.
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Ribosomes and polyribosomes were prepared from bovine thyroid glands. Single ribosomes were similar to those from other mammalian tissues. The distribution of polyribosomes was also similar to that in other tissues. Despite attention to problems of mechanical, enzymatic and chemical breakage, bovine thyroid cells were found to have very few polyribosomes larger than 35 ribosomes, determined by electron microscopy. The heavy fractions consisted in the main of polyribosomes composed of 20 to 30 ribosomes, which are substantially smaller than predicted from the chain molecular weight of the thyroglobulin subunit (165,000) and the MW/ribosome ratio of 3–4000 estimated for other proteins. (Endocrinology83: 1117, 1968)
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