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N. Baichoo, T. Wang, R. Ye, and J.D. Helmann Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon Mol Microbiol 45 2002 1613 1629
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E. Pohl, J.C. Haller, A. Mijovilovich, W. Meyer-Klaucke, E. Garman, and M.L. Vasil Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator Mol Microbiol 47 2003 903 915 The first high resolution structure of Fur in the active, metal-bound form. However, there is considerable diversity in the modes of metal ion recognition within the Fur family. Other family members may bind metals at other sites, not visualized in this structure.
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I. Delany, R. Rappuoli, and V. Scarlato Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis Mol Microbiol 52 2004 1081 1090 This study, together with [19], illustrates the versatility of Fur as a transcriptional regulator.
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Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins
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Q. Que, and J.D. Helmann Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins Mol Microbiol 35 2000 1454 1468
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S.A. Lieser, T.C. Davis, J.D. Helmann, and S.M. Cohen DNA-binding and oligomerization studies of the manganese(II) metalloregulatory protein MntR from Bacillus subtilis Biochemistry 42 2003 12634 12642 Biochemical evidence that the selectivity of MntR for Mn(II) (and Cd) is reflected in the in vitro metal-binding properties of the MntR apo-protein. Unlike DtxR, apo-MntR is a dimer in solution.
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J.A. Imlay Pathways of oxidative damage Annu Rev Microbiol 57 2003 395 418 An excellent overview of the role of Fe-based Fenton chemistry in oxidative damage and a valuable perspective on the major questions motivating current research.
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The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors
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J.D. Helmann, M.F. Wu, A. Gaballa, P.A. Kobel, M.M. Morshedi, P. Fawcett, and C. Paddon The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors J Bacteriol 185 2003 243 253 Provides a global perspective on the role of PerR as a major regulator of adaptive response to low level peroxide stress.
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A.F. Herbig, and J.D. Helmann Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA Mol Microbiol 41 2001 849 859
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A. Changela, K. Chen, Y. Xue, J. Holschen, C.E. Outten, T.V. O'Halloran, and A. Mondragon Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR Science 301 2003 1383 1387 High resolution crystal structure of CueR reveals the molecular basis of Cu(I)-sensing. Remarkably, the two Cys residues that coordinate the bound Cu(I) ion are not conserved in the corresponding B. subtilis CueR protein identified in [39].
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A. Gaballa, M. Cao, and J.D. Helmann Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon Microbiology 149 2003 3413 3421 Identification of CueR as the Cu-sensing MerR homolog responsible for induction of the copZA operon. Unexpectedly, mutation of another MerR homolog also led to greatly reduced induction in response to Cu, apparently due to derepression of a linked multidrug efflux pump. It is speculated that perhaps this pump removes Cu or a Cu complex from the cell, although this model awaits further testing.
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A. Gaballa, and J.D. Helmann Bacillus subtilis CPx-type ATPases: characterization of Cd, Zn, Co and Cu efflux systems Biometals 16 2003 497 505
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Patzer, S.I.1
Hantke, K.2
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