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Structural basis for persulfide-sensing specificity in a transcriptional regulator
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Structural basis for persulfide-sensing specificity in a transcriptional regulator
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Journal Article
Structural basis for persulfide-sensing specificity in a transcriptional regulator
2021
Overview
Cysteine thiol-based transcriptional regulators orchestrate the coordinated regulation of redox homeostasis and other cellular processes by ‘sensing’ or detecting a specific redox-active molecule, which in turn activates the transcription of a specific detoxification pathway. The extent to which these sensors are truly specific in cells for a singular class of reactive small-molecule stressors, for example, reactive oxygen or sulfur species, is largely unknown. Here, we report structural and mechanistic insights into the thiol-based transcriptional repressor SqrR, which reacts exclusively with oxidized sulfur species such as persulfides, to yield a tetrasulfide bridge that inhibits DNA operator–promoter binding. Evaluation of crystallographic structures of SqrR in various derivatized states, coupled with the results of a mass spectrometry-based kinetic profiling strategy, suggest that persulfide selectivity is determined by structural frustration of the disulfide form. These findings led to the identification of an uncharacterized repressor from the bacterial pathogen
Acinetobacter baumannii
as a persulfide sensor.
Structural and kinetic analyses of the transcriptional repressor SqrR in multiple states indicate that its persulfide selectivity is determined by structural frustration in the disulfide form, favoring formation of the tetrasulfide-bridged product.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Acinetobacter baumannii - genetics
/ Acinetobacter baumannii - metabolism
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Chemistry and Materials Science
/ Escherichia coli - metabolism
/ Gene Expression Regulation, Bacterial
/ Genetic Vectors - metabolism
/ Kinetics
/ Protein Conformation, alpha-Helical
/ Protein Conformation, beta-Strand
/ Protein Interaction Domains and Motifs
/ Quinone Reductases - chemistry
/ Quinone Reductases - genetics
/ Quinone Reductases - metabolism
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Sequence Homology, Amino Acid
/ Sulfur
