NDLI: Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription.

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Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription.

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Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Weiss, V. Claverie-martin, F. Magasanik, B.
Description	Author Affiliation: Weiss V ( Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.);
Abstract	We studied the effect of phosphorylation of nitrogen regulator I (NRI) on its binding properties. Both phosphorylated and unphosphorylated NRI bind linearly to a single binding site but cooperatively to two adjacent binding sites. Cooperative binding of NRI is severely affected by phosphorylation: half-maximal binding of NRI-phosphate is at 20-fold lower concentrations than that of unphosphorylated NRI. This is more due to a huge increase in the cooperativity constant--which is the strength of interaction between two NRI dimers--than to an increase in the microscopic binding constant which is the binding affinity to a single binding site. In vitro transcription and DNA footprinting experiments showed that occupation of a single binding site by NRI is not enough for efficient activation and that activation only occurs at a higher NRI concentration. We propose an activation mechanism for NRI in which the phosphorylation of NRI induces a conformational change in the N-terminal domains of the NRI-phosphate dimers, which now interact strongly with each other, leading to a tetramerization of NRI upon binding to two adjacent binding sites. We propose that not the phosphorylation of NRI itself but rather the tetramerization of NRI-phosphate on DNA binding induces the conformational change of the central domain to the active conformation.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	11
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA-Binding Proteins Physiology Escherichia Coli Genetics Gene Expression Regulation, Bacterial Glutamate-Ammonia Ligase Trans-Activators Transcription Factors Bacterial Proteins Metabolism Binding Sites Escherichia Coli Proteins Molecular Sequence Data Oligodeoxyribonucleotides Chemistry PII Nitrogen Regulatory Proteins Phosphorylation Plasmids Protein Binding Regulatory Sequences, Nucleic Acid Transcription, Genetic Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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