Lucarelli, D. and Vasil, M.L. and Meyer-Klaucke, W. and Pohl, E. (2008) 'The metal-dependent regulators FurA and FurB from Mycobacterium tuberculosis.', International journal of molecular sciences., 9 (8). pp. 1548-1560.
The ferric uptake regulators (Fur) form a large family of bacterial metalactivated DNA-binding proteins that control a diverse set of genes at the transcriptional level. Mycobacterium tuberculosis, the causative agent of tuberculosis, expresses two members of the Fur family, designated FurA and FurB. Although both belong to the same family, they share only approximately 25% sequence identity and as a consequence, they differ significantly in some of their key biological functions. FurA appears to be a specialized iron-dependent regulator that controls the katG gene, which encodes for a catalase-peroxidase involved in the response of M. tuberculosis to oxidative stress. KatG is also the key mycobacterial enzyme responsible for the activation of the first-line tuberculosis drug Isoniazid. FurB in contrast requires Zn2+ rather than Fe2+, to bind to its target sequence in regulated genes, which include those involved in Zn2+-homeostasis. Recent biochemical, crystallographic and spectroscopic data have now shed light on the activation and metal discrimination mechanisms in this protein family.
|Keywords:||Metal uptake, Regulator, Ferric, Zinc, Mycobacterium tuberculosis.|
|Full text:||(VoR) Version of Record|
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|Publisher Web site:||http://dx.doi.org/10.3390/ijms9081548|
|Publisher statement:||© 2008 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.|
|Date accepted:||30 July 2008|
|Date deposited:||09 June 2015|
|Date of first online publication:||August 2008|
|Date first made open access:||No date available|
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