Ethyl methanesulfonate-induced mutations of the Sh1 protein in maize.
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Biomedical subjects
Publications and source records attributed to D Schwartz.
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Two ethyl methanesulfonate-induced mutants of the alcohol-dehydrogenase gene in maize have been analyzed. The enzyme subunits produced by the mutants seem to be structurally altered in such a way that the subunit specified by the null allele Adh(1) (0(5657)) does not dimerize with "wild-type" subunits, and that specified by Adh(1) (S(296)) does so only to a limited extent.
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Catabolite repression is defined as the inhibition of enzyme induction by glucose or related substances. In the bacterium E. coli, the effect of glucose appears to be due to a lowering of the cyclic AMP level. A DNA-directed cell-free system for beta-galactosidase synthesis has served as a model system for studying the mechanism of action of cyclic AMP. Previously, it was reported that in this system cyclic AMP is required for normal initiation of mRNA synthesis. A protein factor which acts in conjunction with the cyclic AMP has been partially purified. This protein factor has a high affinity for cyclic AMP. These and other results presented herein lead us to the conclusion that cyclic AMP and a protein factor called the catabolite gene activator protein are part of a positive control system for activating catabolite-sensitive genes.
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The surface areas of the cerebral cortex excluding archipallium of 20 human, 11 cetacean, 6 carnivore, and 5 marsupial brains were determined by stereological methods. There exist rather strict relationships between volume, length of superficially exposed gyri, and cortical surface area.
There are two distinct sets of alcohol dehydrogenase isozymes from maize, but they have subunits in common. Induced mutations at the (Adh(1)) locus altered the migration rate of both Set I and Set II isozymes.
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