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Title: Radiation-induced tetramer-to-dimer transition of Escherichia coli lactose repressor

Abstract

The wild type lactose repressor of Escherichia coli is a tetrameric protein formed by two identical dimers. They are associated via a C-terminal 4-helix bundle (called tetramerization domain) whose stability is ensured by the interaction of leucine zipper motifs. Upon in vitro {gamma}-irradiation the repressor losses its ability to bind the operator DNA sequence due to damage of its DNA-binding domains. Using an engineered dimeric repressor for comparison, we show here that irradiation induces also the change of repressor oligomerisation state from tetramer to dimer. The splitting of the tetramer into dimers can result from the oxidation of the leucine residues of the tetramerization domain.

Authors:
 [1];  [2];  [1]
  1. Centre de Biophysique Moleculaire, CNRS, rue C. Sadron, 45071 Orleans (France)
  2. Department of Radiation Dosimetry, Nuclear Physics Institute AS CR, Na Truhlarce 39/64, 18086, Prague 8 (Czech Republic)
Publication Date:
OSTI Identifier:
22199767
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 386; Journal Issue: 2; Other Information: Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRONMENTAL POLLUTANT EFFECTS ON LIVING ORGANISMS AND BIOLOGICAL MATERIALS; BIOLOGICAL RADIATION EFFECTS; DIMERS; DNA; ESCHERICHIA COLI; GAMMA RADIATION; IN VITRO; IRRADIATION; LACTOSE; LEUCINE; OXIDATION; PROTEINS

Citation Formats

Goffinont, S., Davidkova, M., and Spotheim-Maurizot, M., E-mail: spotheim@cnrs-orleans.fr. Radiation-induced tetramer-to-dimer transition of Escherichia coli lactose repressor. United States: N. p., 2009. Web. doi:10.1016/J.BBRC.2009.06.012.
Goffinont, S., Davidkova, M., & Spotheim-Maurizot, M., E-mail: spotheim@cnrs-orleans.fr. Radiation-induced tetramer-to-dimer transition of Escherichia coli lactose repressor. United States. doi:10.1016/J.BBRC.2009.06.012.
Goffinont, S., Davidkova, M., and Spotheim-Maurizot, M., E-mail: spotheim@cnrs-orleans.fr. Fri . "Radiation-induced tetramer-to-dimer transition of Escherichia coli lactose repressor". United States. doi:10.1016/J.BBRC.2009.06.012.
@article{osti_22199767,
title = {Radiation-induced tetramer-to-dimer transition of Escherichia coli lactose repressor},
author = {Goffinont, S. and Davidkova, M. and Spotheim-Maurizot, M., E-mail: spotheim@cnrs-orleans.fr},
abstractNote = {The wild type lactose repressor of Escherichia coli is a tetrameric protein formed by two identical dimers. They are associated via a C-terminal 4-helix bundle (called tetramerization domain) whose stability is ensured by the interaction of leucine zipper motifs. Upon in vitro {gamma}-irradiation the repressor losses its ability to bind the operator DNA sequence due to damage of its DNA-binding domains. Using an engineered dimeric repressor for comparison, we show here that irradiation induces also the change of repressor oligomerisation state from tetramer to dimer. The splitting of the tetramer into dimers can result from the oxidation of the leucine residues of the tetramerization domain.},
doi = {10.1016/J.BBRC.2009.06.012},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 2,
volume = 386,
place = {United States},
year = {2009},
month = {8}
}