Completing the View of Transcriptional Regulation

Author:

von Hippel Peter H.1

Affiliation:

1. The author is at the Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, OR 97403, USA.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference20 articles.

1. Crystal Structure of the Lactose Operon Repressor and Its Complexes with DNA and Inducer

2. Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes

3. Wild-type lac repressor exists as a tetramer but the “head-groups” of only two subunits at a time bind to an operator or nonspecific DNA site and only these DNA binding domains of the repressor have an important role in the DNA-protein interaction. Hence the dimer of DNA binding domains studied here provides a valid representation of the interactions of the repressor molecule with dsDNA for both the RO and the RD complexes.

4. Studies on the induced synthesis of β-galactosidase in Escherichia coli: The kinetics and mechanism of sulfur incorporation

5. The genetic control and cytoplasmic expression of “Inducibility” in the synthesis of β-galactosidase by E. coli

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