Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum

Kino, Kuniki; Kuratsu, Shoko; Noguchi, Atsushi; Kokubo, Masahiro; Nakazawa, Yozo; Arai, Tomomi; Yagasaki, Makoto; Kirimura, Kohtaro

doi:10.1016/j.bbrc.2006.11.016

Cited by 18 publications

(16 citation statements)

References 25 publications

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“…1). A pathway of glutathione synthesis from cysteine involving a bifunctional glutamate-cysteine ligase/glutathione synthetase is also present as previously proposed [39]. …”

Section: Resultsmentioning

confidence: 99%

Global regulation of gene expression in response to cysteine availability in Clostridium perfringens

et al. 2010

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BackgroundCysteine has a crucial role in cellular physiology and its synthesis is tightly controlled due to its reactivity. However, little is known about the sulfur metabolism and its regulation in clostridia compared with other firmicutes. In Clostridium perfringens, the two-component system, VirR/VirS, controls the expression of the ubiG operon involved in methionine to cysteine conversion in addition to the expression of several toxin genes. The existence of links between the C. perfringens virulence regulon and sulfur metabolism prompted us to analyze this metabolism in more detail.ResultsWe first performed a tentative reconstruction of sulfur metabolism in C. perfringens and correlated these data with the growth of strain 13 in the presence of various sulfur sources. Surprisingly, C. perfringens can convert cysteine to methionine by an atypical still uncharacterized pathway. We further compared the expression profiles of strain 13 after growth in the presence of cystine or homocysteine that corresponds to conditions of cysteine depletion. Among the 177 genes differentially expressed, we found genes involved in sulfur metabolism and controlled by premature termination of transcription via a cysteine specific T-box system (cysK-cysE, cysP1 and cysP2) or an S-box riboswitch (metK and metT). We also showed that the ubiG operon was submitted to a triple regulation by cysteine availability via a T-box system, by the VirR/VirS system via the VR-RNA and by the VirX regulatory RNA.In addition, we found that expression of pfoA (theta-toxin), nagL (one of the five genes encoding hyaluronidases) and genes involved in the maintenance of cell redox status was differentially expressed in response to cysteine availability. Finally, we showed that the expression of genes involved in [Fe-S] clusters biogenesis and of the ldh gene encoding the lactate dehydrogenase was induced during cysteine limitation.ConclusionSeveral key functions for the cellular physiology of this anaerobic bacterium were controlled in response to cysteine availability. While most of the genes involved in sulfur metabolism are regulated by premature termination of transcription, other still uncharacterized mechanisms of regulation participated in the induction of gene expression during cysteine starvation.

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“…1). A pathway of glutathione synthesis from cysteine involving a bifunctional glutamate-cysteine ligase/glutathione synthetase is also present as previously proposed [39]. …”

Section: Resultsmentioning

confidence: 99%

Global regulation of gene expression in response to cysteine availability in Clostridium perfringens

et al. 2010

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“…These include (i) a detailed assessment of the basis for the catalytic promiscuity of E. coli alkaline phosphatase, which can also act as a sulfatase (16); (ii) a new family of lactonases that hydrolyze a variety of lactones, possess low phosphotriesterase activities, and have been shown to be the source of a newly evolved and highly efficient phosphotriesterase (2); (iii) a gentisate dioxygenase that also functions with 1,4-dihydroxy-2-napthoate and salicylate (31); (iv) an ATP-dependent hexokinase from Sulfolobus tokadaii that can phosphorylate glucose, mannose, glucosamine, and N-acetylglucosamine (54); (v) a higher-plant isopropylmalate synthase that not only condenses acetyl coenzyme A (acetyl-CoA) with 2-ketoisovalerate but will also accept 2-oxo acid substrates of two-carbon to six-carbon lengths (19); (vi) a number of variations in the substrate specificities of glutathione synthesis enzymes in comparison to E. coli, Streptococcus agalactiae, and Clostridium acetobutylicum (42); (vii) an amino acid racemase from Pseudomonas putida with an unusual breadth of specificity for amino acids (43); (viii) ATP-forming acetyl-CoA synthetases that accept acetate, propionate, and some longer straight-and branched-chain acyl substrates (32); (ix) an isochorismate pyruvate lyase from Pseudomonas aeruginosa that also has weak chorismate mutase activity (45); and (x) Sulfolobus species that condense pyruvate and aldehydes with two to four carbon atoms (phosphorylated or not) (74). D-2-Hydroxyacid dehydrogenase from Haloferax mediterranei exhibits interesting parallels to the broad-specificity TyrA variants.…”

Section: How Common Is Variation Of Substrate Specificity?mentioning

confidence: 99%

Cohesion Group Approach for Evolutionary Analysis of TyrA, a Protein Family with Wide-Ranging Substrate Specificities

Bonner

Disz

Hwang

et al. 2008

Microbiol Mol Biol Rev

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SUMMARY Many enzymes and other proteins are difficult subjects for bioinformatic analysis because they exhibit variant catalytic, structural, regulatory, and fusion mode features within a protein family whose sequences are not highly conserved. However, such features reflect dynamic and interesting scenarios of evolutionary importance. The value of experimental data obtained from individual organisms is instantly magnified to the extent that given features of the experimental organism can be projected upon related organisms. But how can one decide how far along the similarity scale it is reasonable to go before such inferences become doubtful? How can a credible picture of evolutionary events be deduced within the vertical trace of inheritance in combination with intervening events of lateral gene transfer (LGT)? We present a comprehensive analysis of a dehydrogenase protein family (TyrA) as a prototype example of how these goals can be accomplished through the use of cohesion group analysis. With this approach, the full collection of homologs is sorted into groups by a method that eliminates bias caused by an uneven representation of sequences from organisms whose phylogenetic spacing is not optimal. Each sufficiently populated cohesion group is phylogenetically coherent and defined by an overall congruence with a distinct section of the 16S rRNA gene tree. Exceptions that occasionally are found implicate a clearly defined LGT scenario whereby the recipient lineage is apparent and the donor lineage of the gene transferred is localized to those organisms that define the cohesion group. Systematic procedures to manage and organize otherwise overwhelming amounts of data are demonstrated.

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“…6 In addition, GshF proteins may also be of interest for biotechnological applications for the synthesis of diverse γ-Glu-conjugated dipeptides and tripeptides. 9, 10 We previously proposed that the γ-ECL and GS domains in dimeric GshF from Pasteurella multocida (PmGshF) come together as a distinct set of structural modules connected by an 18-amino-acid linker. 8 In this context, the γ-ECL reaction would be catalyzed by a domain spanning residues 1-462 similar to canonical γ-proteobacterial GshA modules, while the GS activity would be attributed to the C-terminal ATP-grasp-like domain (residues 480-757).…”

Section: Introductionmentioning

confidence: 99%

Glutathione Biosynthesis in Bacteria by Bifunctional GshF Is Driven by a Modular Structure Featuring a Novel Hybrid ATP-Grasp Fold

Stout

Vos

Vergauwen

et al. 2012

Journal of Molecular Biology

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Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum

Cited by 18 publications

References 25 publications

Global regulation of gene expression in response to cysteine availability in Clostridium perfringens

Global regulation of gene expression in response to cysteine availability in Clostridium perfringens

Cohesion Group Approach for Evolutionary Analysis of TyrA, a Protein Family with Wide-Ranging Substrate Specificities

Glutathione Biosynthesis in Bacteria by Bifunctional GshF Is Driven by a Modular Structure Featuring a Novel Hybrid ATP-Grasp Fold

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