The covalent and tertiary structure of bovine liver rhodanese

Ploegman, Jan H.; Drent, Gé; Kalk, Kor H.; Hól, Wim G. J.; Heinrikson, Robert L.; Keim, Philip; Weng, Litai; Russell, John

doi:10.1038/273124a0

Cited by 291 publications

(182 citation statements)

References 41 publications

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“…Rhodanese concentrations were determined using A 280 nm 0.1% ϭ 1.75 (11) and a molecular mass of 33 kDa (12). Rhodanese activity was assayed using a colorimetric method based on the absorbance at 460 nm of the complex formed between the reaction product, thiocyanate, and ferric ion (11).…”

Section: Methodsmentioning

confidence: 99%

Refolding and Reassembly of Active Chaperonin GroEL After Denaturation

Ybarra

Horowitz

1995

Journal of Biological Chemistry

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Conditions are reported that, for the first time, permit the folding and assembly of active chaperonin, GroEL, following denaturation in 8 M urea. The folding could be achieved by dilution or dialysis, and the best yields required the simultaneous presence of ammonium sulfate and the Mg 2؉ complexes of ATP or ADP. Ammonium sulfate was the key to this particular protocol, since there was a small recovery of oligomer in its presence, but no detectable recovery was induced by ATP or ADP without ammonium sulfate. The refolded/reassembled GroEL could arrest the spontaneous folding of rhodanese, and it could participate in the chaperonin-assisted refolding of rhodanese as effectively as GroEL that had never been unfolded. The results demonstrate that the primary sequence of GroEL contains the information required for its folding, assembly, and function. Thus, in contrast to previous studies, although chaperonins may facilitate GroEL folding, they are not necessary for the acquisition of the functional oligomeric state of this chaperone. This ability to fold denatured GroEL in vitro will facilitate studies of the influences that determine the interesting folding pattern adopted by the native protein.

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Section: Methodsmentioning

confidence: 99%

Refolding and Reassembly of Active Chaperonin GroEL After Denaturation

Ybarra

Horowitz

1995

Journal of Biological Chemistry

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“…The rhodanese superfamily members are distinguished by a structural module with an α/β topology in which α-helices surround a central five-stranded β-sheet core (19). At least three variations of the rhodanese domain are found in family members (20).…”

Section: Hydrogen Sulfide (H 2 S)mentioning

confidence: 99%

Thiosulfate sulfurtransferase-like domain–containing 1 protein interacts with thioredoxin

Libiad

Motl

Akey

et al. 2018

Journal of Biological Chemistry

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ǂ These authors contributed equally to this work Rhodanese domains are structural modules present in the sulfurtransferase superfamily. These domains can exist as single units, in tandem repeats or fused to domains with other activities. Despite their prevalence across species, the specific physiological roles of most sulfurtransferases are not known. Mammalian rhodanese and mercaptopyruvate sulfurtransferase are perhaps the best-studied members of this protein superfamily and are involved in hydrogen sulfide metabolism. The relatively unstudied human thiosulfate sulfurtransferase like domain-containing 1 (TSTD1) protein, a single-domain cytoplasmic sulfurtransferase, was also postulated to play a role in the sulfide oxidation pathway using thiosulfate to form glutathione persulfide, for subsequent processing in the mitochondrial matrix. Prior kinetic analysis of TSTD1 was performed at pH 9.2, raising questions about relevance and the proposed model for TSTD1 function. In this study, we report a 1.04 Å resolution crystal structure of human TSTD1, which displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase. Kinetic studies with a combination of sulfur donors and acceptors reveal that TSTD1 exhibits a low K M for thioredoxin as a sulfane sulfur acceptor and that it utilizes thiosulfate inefficiently as a sulfur donor. The active site exposure and its interaction with thioredoxin, suggest that TSTD1 might play a role in sulfide-based signaling. The apical localization of TSTD1 in human colonic crypts, which interfaces with sulfide-releasing microbes, and the overexpression of TSTD1 in colon cancer, provides potentially intriguing clues as to its role in sulfide metabolism. Hydrogen sulfide (H 2 S)1 is an important signaling molecule with effects on multiple physiological processes including neuromodulation, inflammation and cardiac function (1-7). Maintaining healthy levels of H 2 S in mammalian cells requires tight control of its biosynthesis and its catabolism (8,9). H 2 S is produced endogenously by two enzymes in the transsulfuration pathway, cystathionine β-synthase and γ-cystathionase as well as by mercaptopyruvate sulfurtransferase (MST) (10-13). H 2 S is oxidized via the sulfide oxidation pathway to generate the end-products thiosulfate Protein persulfidation, a posttranslational modification of cysteine residues, is postulated to be a major mechanism by which H 2 S signals (17). However, the mechanism by which target proteins acquire this modification and the sulfur source(s) used in persulfidation reactions are unclear (18). Sulfurtransferases like rhodanese or the single rhodanese domain containing TSTD1 could potentially play a role in protein persulfidation because of their capacity to form an active site cysteine persulfide during their reaction cycle (18).The rhodanese superfamily members are distinguished by a structural module with an α/β topology in which α-helices surround a central five-stranded β-sheet core (19). At least three variations...

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“…The tertiary structure of bovine rhodanese is composed of two domains which, in spite of negligible sequence homology, are characterized by very similar three-dimensional folds; the two domains are connected by a loop at the surface of the molecule Ploegman et al, 1978). The active site is located in the C-terminal domain, near the interface between the two domains.…”

Section: Introductionmentioning

confidence: 99%