REPRESSION-DEPENDENT ALTERATION OF AN ARGININE ENZYME IN Escherichia coli
- 1 October 1969
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 64 (2), 686-692
- https://doi.org/10.1073/pnas.64.2.686
Abstract
Treatment of susceptible Escherichia coli K12 derivatives with 0.4 M Mg(++) at 37 degrees , potentiated by L-arginine or L-canavanine, leads to alteration of acetylornithine delta-transaminase. The alteration, obtained in the absence of protein synthesis and reversible at 0 or 37 degrees , is manifested in extracts by lowered activity and modified substrate affinity behavior of the enzyme without gross changes in sedimentation properties. Cells grown under arginine repression are susceptible to the treatment; cells grown under genetic or steady-state physiological derepression are not. Transaminase synthesized during early derepression can be altered, although to progressively diminishing extents. Enzyme formed under steady-state derepression becomes alterable following transition to repression. The Mg(++) -dependent alteration can be thought to arise while the enzyme, arginine (or canavanine), and aporepressor are in contact, and to reflect a physiological process such as the participation of the enzyme in the repressive complex.Keywords
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