PspE (phage‐shock protein E) of <i>Escherichia coli</i> is a rhodanese

Adams, Hendrik; Teertstra, Wieke R.; Koster, Margot; Tommassen, Jan

doi:10.1016/s0014-5793(02)02695-9

Cited by 52 publications

(59 citation statements)

References 39 publications

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“…Nevertheless, a picture is starting to emerge of an enzyme activity that is up-regulated in response to stress. Rhodanese and proteins containing rhodanese-like domains are implicated in response to heat shock, phage shock, and senescence (13,23). MSTs have been implicated in the management of oxidative stress (27,28), and the trypanosomatid LmMST is also linked to cysteine biosynthesis (27).…”

Section: Resultsmentioning

confidence: 99%

“…For example, sulfurtransferases may be involved in the formation and maintenance of iron-sulfur clusters in protein (4,5), detoxification of cyanide (6,7), degradation of cysteine (8), biosynthesis of the molybdopterin cofactor of xanthine oxidase (9), selenium metabolism (2,10), and thiamine and 4-thiouridine biosynthesis (11,12). The expression of specific sulfurtransferases is up-regulated under conditions of peroxide or hypo-sulfur stress, osmotic shock, and phage infection (13), suggesting that such enzyme activity is protective of the cell and/or involved in repair processes. Nevertheless, despite intensive study, the biological functions and identification of the physiological substrates of sulfurtransferases remain uncertain.…”

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confidence: 99%

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The Crystal Structure of Leishmania major 3-Mercaptopyruvate Sulfurtransferase

Alphey

Williams

Mottram

et al. 2003

Journal of Biological Chemistry

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Leishmania major 3-mercaptopyruvate sulfurtransferase is a crescent-shaped molecule comprising three domains. The N-terminal and central domains are similar to the thiosulfate sulfurtransferase rhodanese and create the active site containing a persulfurated catalytic cysteine (Cys-253) and an inhibitory sulfite coordinated by Arg-74 and Arg-185. A serine protease-like triad, comprising Asp-61, His-75, and Ser-255, is near Cys-253 and represents a conserved feature that distinguishes 3-mercaptopyruvate sulfurtransferases from thiosulfate sulfurtransferases. During catalysis, Ser-255 may polarize the carbonyl group of 3-mercaptopyruvate to assist thiophilic attack, whereas Arg-74 and Arg-185 bind the carboxylate group. The enzyme hydrolyzes benzoyl-Arg-p-nitroanilide, an activity that is sensitive to the presence of the serine protease inhibitor N ␣ -p-tosyl-L-lysine chloromethyl ketone, which also lowers 3-mercaptopyruvate sulfurtransferase activity, presumably by interference with the contribution of Ser-255. The L. major 3-mercaptopyruvate sulfurtransferase is unusual with an 80-amino acid C-terminal domain, bearing remarkable structural similarity to the FK506-binding protein class of peptidylprolyl cis/trans-isomerase. This domain may be involved in mediating protein folding and sulfurtransferase-protein interactions.Sulfurtransferases (EC 2.8.1.1-5) catalyze the transfer of sulfane sulfur from a donor molecule to a thiophilic acceptor. These enzymes are widely distributed in plants, animals, and bacteria (1-3) and have been implicated in a wide range of biological processes. For example, sulfurtransferases may be involved in the formation and maintenance of iron-sulfur clusters in protein (4, 5), detoxification of cyanide (6, 7), degradation of cysteine (8), biosynthesis of the molybdopterin cofactor of xanthine oxidase (9), selenium metabolism (2, 10), and thiamine and 4-thiouridine biosynthesis (11,12). The expression of specific sulfurtransferases is up-regulated under conditions of peroxide or hypo-sulfur stress, osmotic shock, and phage infection (13), suggesting that such enzyme activity is protective of the cell and/or involved in repair processes. Nevertheless, despite intensive study, the biological functions and identification of the physiological substrates of sulfurtransferases remain uncertain.The archetypal sulfurtransferase is rhodanese, a thiosulfate: cyanide sulfurtransferase (TST) 1 able to catalyze the transfer of the thiosulfate sulfur to cyanide in vitro. The related 3-mercaptopyruvate sulfurtransferase (3-mercaptopyruvate:cyanide sulfurtransferase (MST)), first discovered in rat liver (14), catalyzes reactions similar to those catalyzed by rhodanese, but uses 3-mercaptopyruvate in preference to thiosulfate as the donor in the two-step reaction,where E represents the free enzyme and ES the enzyme-sulfur adduct.Crystal structures of rhodaneses have been elucidated and analyzed in detail (15)(16)(17)(18)(19)(20). The enzyme consists of two domains that, despite a low level of sequence iden...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

The Crystal Structure of Leishmania major 3-Mercaptopyruvate Sulfurtransferase

Alphey

Williams

Mottram

et al. 2003

Journal of Biological Chemistry

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“…Interestingly, structural and functional studies performed on the E. coli TST GlpE, containing a single 108-amino acid rhodanese domain, demonstrated that a single domain can be selfsufficient for thiocyanate formation from thiosulfate in the presence of cyanide (15) Single catalytic rhodanese domain proteins are encoded by both eukaryotic and prokaryotic genomes. These proteins have been associated with specific stress conditions as in the case of the Drosophyla melanogaster heat shock protein 67-B2, of the E. coli phage-shock protein E (PspE) (16), and of the Vibrio cholerae shock protein Q9KN65 (17). Proteins containing single rhodanese domain have also been associated with the process of leaf senescence in plants.…”

Section: Group I: Single Domain Proteinsmentioning

confidence: 99%

Common themes and variations in the rhodanese superfamily

2007

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SummaryThe rhodanese homology domain is a ubiquitous fold found in several phylogenetically related proteins encoded by eubacterial, archeal, and eukaryotic genomes. Although rhodanese-like proteins share evolutionary relationships, analysis of their sequences highlights that they are so heterogeneous to form the rhodanese superfamily. The variability occurs at different levels including sequence, active site loop length, presence of a critical catalytic Cys residue, and domain arrangement. Even within the same genome, multiple genes encode rhodanese-like proteins presenting with variably arranged rhodanese domain(s): as single or tandem domain(s), or combined with other protein domain(s). Given the highly variable organization of the rhodanese domain(s) and the context where it is found, here we review the structural organization and function of the rhodanese-like proteins. The overview of the most recent findings about rhodanese allow us to depict a superfamily of versatile proteins relying on persulfide chemistry to accomplish cellular functions spanning from resistance to environmental threats, such as cyanide, and key cellular reactions related to sulfur metabolism and progression of cell cycle. IUBMB Life, 59: 51-59, 2007

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“…The rhodanese homology domain has a conserved cysteine residue that participates in catalysis (12). The ϳ110-amino acid rhodanese domain may comprise the entire protein, as in the GlpE and PspE rhodaneses of E. coli (13,14), or the domain may be fused to other protein domains of known or unknown function. Other rhodaneses and mercaptopyruvate sulfurtransferases contain two rhodanese homology domains, but only the C-terminal domain contains an active site cysteine that participates in catalysis (12).…”

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Functional Diversity of the Rhodanese Homology Domain

Wolfe

Ahmed

Lacourciere

et al. 2004

Journal of Biological Chemistry

103

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Escherichia coli has eight genes predicted to encode sulfurtransferases having the active site consensus sequence Cys-Xaa-Xaa-Gly. One of these genes, ybbB, is frequently found within bacterial operons that contain selD, the selenophosphate synthetase gene, suggesting a role in selenium metabolism. We show that ybbB is required in vivo for the specific substitution of selenium for sulfur in 2-thiouridine residues in E. coli tRNA. This modified tRNA nucleoside, 5-methylaminomethyl-2-selenouridine (mnm 5 se 2 U), is located at the wobble position of the anticodons of tRNA Lys , tRNA Glu , and tRNA 1Gln . Nucleoside analysis of tRNAs from wild-type and ybbB mutant strains revealed that production of mnm 5 se 2 U is lost in the ybbB mutant but that 5-methylaminomethyl-2-thiouridine, the mnm 5 se 2 U precursor, is unaffected by deletion of ybbB. Thus, ybbB is not required for the initial sulfurtransferase reaction but rather encodes a 2-selenouridine synthase that replaces a sulfur atom in 2-thiouridine in tRNA with selenium. Purified 2-selenouridine synthase containing a C-terminal His 6 tag exhibited spectral properties consistent with tRNA bound to the enzyme. In vitro mnm 5 se 2 U synthesis is shown to be dependent on 2-selenouridine synthase, SePO 3 , and tRNA. Finally, we demonstrate that the conserved Cys 97 (but not Cys 96 ) in the rhodanese sequence motif Cys 96 -Cys 97 -Xaa-Xaa-Gly is required for 2-selenouridine synthase in vivo activity. These data are consistent with the ybbB gene encoding a tRNA 2-selenouridine synthase and identifies a new role for the rhodanese homology domain in enzymes.

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PspE (phage‐shock protein E) of Escherichia coli is a rhodanese

Cited by 52 publications

References 39 publications

The Crystal Structure of Leishmania major 3-Mercaptopyruvate Sulfurtransferase

The Crystal Structure of Leishmania major 3-Mercaptopyruvate Sulfurtransferase

Common themes and variations in the rhodanese superfamily

Functional Diversity of the Rhodanese Homology Domain

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