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Review
. 2004 Apr;186(7):1911-8.
doi: 10.1128/JB.186.7.1911-1918.2004.

Spx-RNA polymerase interaction and global transcriptional control during oxidative stress

Peter Zuber  1
Affiliations
Review

Spx-RNA polymerase interaction and global transcriptional control during oxidative stress

Peter Zuber. J Bacteriol. 2004 Apr.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Positive transcriptional regulation of a two-component signal transduction system and negative control exerted by the Spx protein. The histidine protein kinase (membrane-bound HPK sensor) autophosphorylates in response to a stimulus (i.e., ComX) and donates the phosphate to the response regulator (RR activator), which then interacts with a promoter region of a gene under its control. Spx is degraded by the protease ClpXP, allowing transcriptional activation to proceed. The subunits of RNAP, β, β′, α, and σ, are indicated, as is the location of the αCTD. Upon disulfide stress or in either a clpX or clpP mutant, Spx accumulates and binds to the αCTD and blocks the activator-RNAP interaction.
FIG. 2.
FIG. 2.
(A) Amino acid sequence of Spx and the sites of the CXXC motif, the conserved G residue that is the site of the Spxcxs-16 substitution, and the DD substitution at the extreme C terminus that renders Spx insensitive to ClpXP proteolysis. The boldface type indicates the regions of sequence identity shared by the Spx orthologs. The secondary structure predictions (50) for Spx and the E. coli R773 ArsC protein were determined, and the structures were aligned (H, α helix; S, β strand; C, coil). The four conserved β strands that form the mixed β sheet are indicated. (B) Structural representation of the ArsC protein with the C-terminal region (where homology with Spx departs) omitted. The positions of the conserved Cys10 residue, the Gly52 residue, and the four-strand mixed β sheet (yellow) are indicated.
FIG. 3.
FIG. 3.
Conservation in the low-G+C-content gram-positive bacteria of the spx locus, showing the tight linkage with the mecA gene (not observed in streptococci). The arrows represent genes and their orientations; the conserved genes of the locus are indicated by shaded arrows.
FIG. 4.
FIG. 4.
Alignment of the amino acid sequences of the RNAP αCTD of gram-positive (top) and gram-negative (bottom) species that include helix 1 and the adjacent sequence in the αCTD. The V and Y residue positions are the sites of the rpoAcxs amino acid substitutions.
See this image and copyright information in PMC

References

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