Involvement of the RNA polymerase α subunit <i>C</i>‐terminal region in co‐operative interaction and transcriptional activation with OxyR protein

Tao, Kazuyuki; Fujita, Nobuyuki; Ishihama, Akira

doi:10.1111/j.1365-2958.1993.tb01176.x

Cited by 72 publications

(59 citation statements)

References 16 publications

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“…BenM bound to Site 2 could activate transcription via contacts with RNA polymerase, as occurs for Class I activators (9,23,(31)(32)(33)(34). Consistent with a Class I type of activation, the Ϫ35 region of benA does not match the consensus for promoters with high affinity for RNA polymerase.…”

Section: Benm Is Tetramericmentioning

confidence: 86%

Synergistic transcriptional activation by one regulatory protein in response to two metabolites

Bundy

Collier

Hoover

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

129

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BenM is a LysR-type bacterial transcriptional regulator that controls aromatic compound degradation in Acinetobacter sp. ADP1. Here, in vitro transcription assays demonstrated that two metabolites of aromatic compound catabolism, benzoate and cis,cismuconate, act synergistically to activate gene expression. The level of BenM-regulated benA transcription was significantly higher in response to both compounds than the combined levels due to each alone. These compounds also were more effective together than they were individually in altering the DNase I footprint patterns of BenM-DNA complexes. This type of dual-inducer synergy provides great potential for rapid and large modulations of gene expression and may represent an important, and possibly widespread, feature of transcriptional control.

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Section: Benm Is Tetramericmentioning

confidence: 86%

Synergistic transcriptional activation by one regulatory protein in response to two metabolites

Bundy

Collier

Hoover

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

129

View full text Add to dashboard Cite

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“…Two LysR-type proteins, TrpI and OxyR, are known to be class I activators (14,21,42), and the Cys Ϫ phenotype of two rpoA mutants (encoding the ␣ subunit) suggests that CysB is also a member of this group (11,27). In addition, Bennett and Shi (2) have found that cysB is required for efficient expression of adi, the gene for a biodegradative arginine decarboxylase of E. coli, and that this process is defective in a strain containing one of these mutations, rpoA341, which results in an Glu-toLys change at amino acid residue 271 (44).…”

Section: Discussionmentioning

confidence: 99%

Hydroxyl radical footprints and half-site arrangements of binding sites for the CysB transcriptional activator of Salmonella typhimurium

Hryniewicz

Kredich

1995

J Bacteriol

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CysB is a transcriptional activator for the cysteine regulon and negatively autoregulates its own gene, cysB. Transcription activation also requires an inducer, N-acetyl-L-serine. CysB is known to bind to activation sites just upstream of the ؊35 regions of the positively regulated cysJIH, cysK, and cysP promoters and to a repressor site centered at about ؉1 in the cysB promoter. Additional accessory sites have been found in positively regulated promoters. The hydroxyl radical footprinting experiments reported here indicate that the activation sites CBS-J1, CBS-K1, and CBS-P1 in the cysJIH, cysK, and cysP promoters are composed of two convergently oriented 19-bp half-sites separated by 1 or 2 bp. N-Acetyl-L-serine stimulates binding to these sites as well as to the accessory sites CBS-J2 and CBS-P2, both of which share a similar topology with activation sites. A second topology is found in the accessory site CBS-K2 and the repressor site CBS-B, which contain divergently oriented 19-bp half-sites separated by one or two helical turns. N-Acetyl-L-serine inhibits binding to these two sites. A third topology is present in the cysK and cysP promoters, where an additional half-site is oriented toward the activation site and separated from it by one helical turn. Here, CysB binds to all three half-sites, bending the DNA, and N-acetyl-L-serine decreases the extent of bending. The marked dissimilarities of these half-site arrangements and of their responses to N-acetyl-L-serine suggest that CysB, a homotetramer, binds to them with different combinations of subunits.

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“…The OxyR protein belongs to the LysR family of transcription factors. Under activating conditions it binds as a tetramer near the −35 region of at least 20 regulon members (42) ( Table 2), and it stimulates transcription through direct contact with RNA polymerase (43). Activation by H 2 O 2 occurs through the oxidation of the Cys-199 residue to a sulfenic acid form.…”

Section: The Oxyr and Perr Regulators Of Responses To H 2 O 2 Stressmentioning

confidence: 99%

Cellular Defenses against Superoxide and Hydrogen Peroxide

Imlay

2008

Annu. Rev. Biochem.

1,335

1,310

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Life evolved in an anaerobic world; therefore, fundamental enzymatic mechanisms and biochemical pathways were refined and integrated into metabolism in the absence of any selective pressure to avoid reactivity with oxygen. After photosystem 2 appeared, environmental oxygen levels rose very slowly. During this time microorganisms acquired oxygen tolerance by jettisoning enzymes that use glycyl radicals and low-potential iron-sulfur clusters, which can be directly poisoned by oxygen. They also developed mechanisms to defend themselves against O 2 − and hydrogen peroxide, partially reduced oxygen species that are generated as inadvertent by-products of aerobic metabolism. These species are more chemically reactive than is molecular oxygen itself. Contemporary organisms have inherited both the vulnerabilities and the defenses of these ancestral microbes. Current research seeks to identify these, and bacteria comprise an exceptionally accessible experimental system that has provided the many of the answers. This manuscript reviews recent developments and identifies remaining puzzles.

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Involvement of the RNA polymerase α subunit C‐terminal region in co‐operative interaction and transcriptional activation with OxyR protein

Cited by 72 publications

References 16 publications

Synergistic transcriptional activation by one regulatory protein in response to two metabolites

Synergistic transcriptional activation by one regulatory protein in response to two metabolites

Hydroxyl radical footprints and half-site arrangements of binding sites for the CysB transcriptional activator of Salmonella typhimurium

Cellular Defenses against Superoxide and Hydrogen Peroxide

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