Conformational analysis and chemical reactivity of the multidomain sulfurtransferase, Staphylococcus aureus CstA

Biochemistry
Khadine A HigginsDavid P Giedroc

Abstract

The cst operon of the major human pathogen Staphylococcus aureus (S. aureus) is under the transcriptional control of CsoR-like sulfurtransferase repressor (CstR). Expression of this operon is induced by hydrogen sulfide, and two components of the cst operon, cstA and cstB, protect S. aureus from sulfide toxicity. CstA is a three-domain protein, and each domain harbors a single cysteine that is proposed to function in vectorial persulfide shuttling. We show here that single cysteine substitution mutants of CstA fail to protect S. aureus against sulfide toxicity in vivo. The N-terminal domain of CstA exhibits thiosulfate sulfurtransferase (TST; rhodanese) activity, and a Cys66 (34)S-persulfide is formed as a catalytic intermediate in both the presence and absence of the adjacent TusA-like domain using (34)S-SO3(2-) as a substrate. Cysteine persulfides can be trapped on both C66 in CstA(Rhod) and on C66 and C128 in CstA(Rhod-TusA) when incubated with thiosulfate, sodium tetrasulfide (Na2S4), and in situ persulfurated SufS. C66A substitution in CstA(Rhod-TusA) abolishes C128 S-sulfhydration, consistent with directional persulfide shuttling in CstA. Fully reduced CstA(Rhod-TusA) is predominately monomeric, and high resolution tandem...Continue Reading

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Citations

Jun 15, 2017·Molecular Microbiology·David P Giedroc
Jul 24, 2020·The Journal of Biological Chemistry·Brenna J C Walsh, David P Giedroc
Feb 16, 2017·Proceedings of the National Academy of Sciences of the United States of America·Takayuki ShimizuShinji Masuda
Oct 31, 2018·Frontiers in Microbiology·Hui PengDavid P Giedroc
Aug 7, 2019·Journal of Biochemistry·Takayuki Shimizu, Shinji Masuda
Feb 6, 2021·Biological Chemistry·Nico LinznerHaike Antelmann

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