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72 residues of gal repressor fused to beta-galactosidase repress the gal operon of E. coli

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Koenen,  Michael
Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society;
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

von Wilcken−Bergmann, B., Koenen, M., Griesser, H. W., & Müller−Hill, B. (1983). 72 residues of gal repressor fused to beta-galactosidase repress the gal operon of E. coli. EMBO Journal, 2(8), 1271-1274. doi:10.1002/j.1460-2075.1983.tb01580.x.


Cite as: http://hdl.handle.net/21.11116/0000-0000-D86F-1
Abstract
An active gene has been constructed which produces a chimera consisting of the N-terminal domain of the gal repressor and all but the first five residues of beta-galactosidase. Seventy two residues of gal repressor fused to beta-galactosidase as tetrameric core are sufficient to repress the gal operon in vivo and to bind to the gal operator in vitro.