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Asymmetric allosteric activation of the symmetric ArgR hexamer

Jin, L H; Xue, Wei-Feng LU ; Fukayama, J W; Yetter, J; Pickering, M and Carey, J (2005) In Journal of Molecular Biology 346(1). p.43-56
Abstract
Hexameric arginine repressor, ArgR, bound to L-arginine serves both as the master transcriptional repressor/activator at diverse regulons in a wide range of bacteria and as a required cofactor for resolution of ColE1 plasmid multimers. Multifunctional ArgR is thus unusual in possessing features of specific gene regulators, global regulators, and non-specific gene organizers; its closest functional analog is probably CAP, the cyclic AMP receptor/activator protein. Isothermal titration calorimetry, surface plasmon resonance, and proteolysis indicate that binding of a single L-arginine residue per ArgR hexamer triggers a global conformational change and resets the affinities of the remaining five sites, making them 100-fold weaker. The... (More)
Hexameric arginine repressor, ArgR, bound to L-arginine serves both as the master transcriptional repressor/activator at diverse regulons in a wide range of bacteria and as a required cofactor for resolution of ColE1 plasmid multimers. Multifunctional ArgR is thus unusual in possessing features of specific gene regulators, global regulators, and non-specific gene organizers; its closest functional analog is probably CAP, the cyclic AMP receptor/activator protein. Isothermal titration calorimetry, surface plasmon resonance, and proteolysis indicate that binding of a single L-arginine residue per ArgR hexamer triggers a global conformational change and resets the affinities of the remaining five sites, making them 100-fold weaker. The analysis suggests a novel thermodynamic signature for this mechanism of activation. (C) 2004 Elsevier Ltd. All rights reserved. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Journal of Molecular Biology
volume
346
issue
1
pages
43 - 56
publisher
Elsevier
external identifiers
  • pmid:15663926
  • wos:000226674900005
  • scopus:12344307390
ISSN
1089-8638
DOI
10.1016/j.jmb.2004.11.031
language
English
LU publication?
yes
id
2287060d-f610-4975-84c7-5b533d1d92ba (old id 151566)
date added to LUP
2007-06-29 11:18:14
date last changed
2017-01-01 06:45:39
@article{2287060d-f610-4975-84c7-5b533d1d92ba,
  abstract     = {Hexameric arginine repressor, ArgR, bound to L-arginine serves both as the master transcriptional repressor/activator at diverse regulons in a wide range of bacteria and as a required cofactor for resolution of ColE1 plasmid multimers. Multifunctional ArgR is thus unusual in possessing features of specific gene regulators, global regulators, and non-specific gene organizers; its closest functional analog is probably CAP, the cyclic AMP receptor/activator protein. Isothermal titration calorimetry, surface plasmon resonance, and proteolysis indicate that binding of a single L-arginine residue per ArgR hexamer triggers a global conformational change and resets the affinities of the remaining five sites, making them 100-fold weaker. The analysis suggests a novel thermodynamic signature for this mechanism of activation. (C) 2004 Elsevier Ltd. All rights reserved.},
  author       = {Jin, L H and Xue, Wei-Feng and Fukayama, J W and Yetter, J and Pickering, M and Carey, J},
  issn         = {1089-8638},
  language     = {eng},
  number       = {1},
  pages        = {43--56},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Biology},
  title        = {Asymmetric allosteric activation of the symmetric ArgR hexamer},
  url          = {http://dx.doi.org/10.1016/j.jmb.2004.11.031},
  volume       = {346},
  year         = {2005},
}