Abstract
A specific, high affinity, IAA binding site was demonstrated in both a cytosolic fraction, and in isolated nuclei, fromNicotiana tabacum cv. Wisconsin No. 38 cells grown in suspension culture. The amount of the binding site detected in both these fractions changed during the culture cycle according to a strict pattern. The molecular mass of the binding site was estimated by gel filtration to be approximately 175 000 and it appears to be a protein. When partially purified by affinity chromatography and allowed to pre-incubate with IAA, the site had a significant stimulatory effect on total RNA synthesis, as measured by a cell-free assay system. Unpurified extracts had no such effects. The system behaves rather like the steroid hormone-receptor system in animals.
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