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SurR regulates hydrogen production in Pyrococcus furiosus by a sulfur‐dependent redox switch
Author(s) -
Yang Hua,
Lipscomb Gina L.,
Keese Annette M.,
Schut Gerrit J.,
Thomm Michael,
Adams Michael W. W.,
Wang Bi Cheng,
Scott Robert A.
Publication year - 2010
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2010.07275.x
Subject(s) - pyrococcus furiosus , biology , gene , derepression , biochemistry , hydrogenase , operon , sulfur metabolism , transcription (linguistics) , redox , microbiology and biotechnology , gene expression , escherichia coli , enzyme , psychological repression , chemistry , archaea , linguistics , philosophy , organic chemistry
Summary We present structural and biochemical evidence for a redox switch in the archaeal transcriptional regulator SurR of Pyrococcus furiosus , a hyperthermophilic anaerobe. P. furiosus produces H 2 during fermentation, but undergoes a metabolic shift to produce H 2 S when elemental sulfur (S 0 ) becomes available. Changes in gene expression occur within minutes of S 0 addition, and the majority of these S 0 ‐responsive genes are regulatory targets of SurR, a key regulator involved in primary S 0 response. SurR was shown in vitro to have dual functionality, activating transcription of some of these genes, notably the hydrogenase operons, and repressing others, including a gene‐encoding sulfur reductase. This work demonstrates via biochemical and structural evidence that the activity of SurR is modulated by cysteine residues in a CxxC motif that constitutes a redox switch. Oxidation of the switch with S 0 inhibits sequence‐specific DNA binding by SurR, leading to deactivation of genes related to H 2 production and derepression of genes involved in S 0 metabolism.