Asymmetric allosteric activation of the symmetric ArgR hexamer
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/151566
- author
- Jin, L H ; Xue, Wei-Feng LU ; Fukayama, J W ; Yetter, J ; Pickering, M and Carey, J
- organization
- publishing date
- 2005
- 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
- 2016-04-01 15:44:19
- date last changed
- 2022-01-28 06:49:28
@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}},
doi = {{10.1016/j.jmb.2004.11.031}},
volume = {{346}},
year = {{2005}},
}