2-Oxoaldehyde metabolism in microorganisms

1989 ◽  
Vol 35 (4) ◽  
pp. 423-431 ◽  
Author(s):  
Kousaku Murata ◽  
Yoshiharu Inoue ◽  
Hae-ik Rhee ◽  
Akira Kimura
Keyword(s):  
Yeast Cells ◽  
Glyoxalase I ◽  
Glyoxalase System ◽  
Metabolizing Enzymes ◽  
Phenotypic Characters ◽  
Metabolism Regulation ◽  
Eukaryotic Microorganisms ◽  
Reductase Gene ◽  
Dividing Cells ◽  
I Gene

The properties of methylglyoxal-metabolizing enzymes in prokaryotic and eukaryotic microorganisms were studied systematically and compared with those of mammalian enzymes. The enzymes constitute a glycolytic bypass and convert methylglyoxal into pyruvate via lactate. The first step in this conversion is catalyzed by glyoxalase I, methylglyoxal reductase, or methylglyoxal dehydrogenase. The regulation of the yeast glyoxalase system was analyzed. The system was closely related to the proliferative states of yeast cells, the activity of the system being high in dividing cells and low in nondividing ones. The gene for the glyoxalase I of Pseudomonas putida and the genes responsible for the activity of glyoxalase I and methylglyoxal reductase in Saccharomyces cerevisiae were cloned and their structural and phenotypic characters studied.Key words: 2-oxoaldehydes metabolism, regulation of glyoxalase system, cloning, glyoxalase I gene, methylglyoxal reductase gene, methylglyoxal metabolism.

scholarly journals Heterologous expression of a Glyoxalase I gene from sugarcane confers tolerance to several environmental stresses in bacteria

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e5873 ◽  
Author(s):  
Qibin Wu ◽  
Shiwu Gao ◽  
Yong-Bao Pan ◽  
Yachun Su ◽  
Michael P. Grisham ◽  
...  
Keyword(s):  
Abiotic Stresses ◽  
Plasmid Vector ◽  
Stress Conditions ◽  
Glyoxalase I ◽  
Glyoxalase System ◽  
Biotic And Abiotic Stresses ◽  
Expression Plasmid ◽  
Reading Frame ◽  
E Coli ◽  
I Gene

Glyoxalase I belongs to the glyoxalase system that detoxifies methylglyoxal (MG), a cytotoxic by-product produced mainly from triose phosphates. The concentration of MG increases rapidly under stress conditions. In this study, a novel glyoxalase I gene, designated as SoGloI was identified from sugarcane. SoGloI had a size of 1,091 bp with one open reading frame (ORF) of 885 bp encoding a protein of 294 amino acids. SoGloI was predicted as a Ni2+-dependent GLOI protein with two typical glyoxalase domains at positions 28–149 and 159–283, respectively. SoGloI was cloned into an expression plasmid vector, and the Trx-His-S-tag SoGloI protein produced in Escherichia coli was about 51 kDa. The recombinant E. coli cells expressing SoGloI compared to the control grew faster and tolerated higher concentrations of NaCl, CuCl2, CdCl2, or ZnSO4. SoGloI ubiquitously expressed in various sugarcane tissues. The expression was up-regulated under the treatments of NaCl, CuCl2, CdCl2, ZnSO4 and abscisic acid (ABA), or under simulated biotic stress conditions upon exposure to salicylic acid (SA) and methyl jasmonate (MeJA). SoGloI activity steadily increased when sugarcane was subjected to NaCl, CuCl2, CdCl2, or ZnSO4 treatments. Sub-cellular observations indicated that the SoGloI protein was located in both cytosol and nucleus. These results suggest that the SoGloI gene may play an important role in sugarcane’s response to various biotic and abiotic stresses.

Characterization of the glyoxalase I gene from the vascular wilt fungus Verticillium dahliae

2006 ◽  
Vol 52 (9) ◽  
pp. 816-822 ◽  
Author(s):  
A Klimes ◽  
M J Neumann ◽  
S J Grant ◽  
K F Dobinson
Keyword(s):  
Verticillium Dahliae ◽  
Glyoxalase I ◽  
Vascular Wilt ◽  
Glyoxalase System ◽  
Enhanced Sensitivity ◽  
Acid Protein ◽  
Gene Homologue ◽  
I Gene ◽  
Amino Acid Protein

A glyoxalase I gene homologue (VdGLO1) was identified in the vascular wilt fungus Verticillium dahliae by sequence tag analysis of genes expressed during resting structure development. The results of the current study show that the gene encodes a putative 345 amino acid protein with high similarity to glyoxalase I, which produces S-D-lactoylglutathione from the toxic metabolic by-product methylglyoxal (MG). Disruption of the V. dahliae gene by Agrobacterium tumefaciens-mediated transformation resulted in enhanced sensitivity to MG. Mycelial growth of disruption mutants was severely reduced in the presence of 5 mmol/L MG. In contrast, spore production in liquid medium was abolished at 1 mmol/L MG, although not at physiologically relevant concentrations of ≤100 µmol/L. In this first report on the characterization of a glyoxalase I gene in a vascular wilt pathogen, we found that disruption of VdGLO1 had no discernable effect on the pathogenicity of V. dahliae. These data suggest that while the glyoxalase system is necessary for effectively dealing with catastrophic levels of MG, under normal conditions of growth and infection, other MG detoxification pathways in V. dahliae are able to compensate for the absence of the glyoxalase system.Key words: verticillium wilt, glycolytic methylglyoxal pathway, 2-oxoaldehydes.

Receptor for advanced glycation end products (RAGE) and glyoxalase I gene polymorphisms in pathological pregnancy

2012 ◽  
Vol 45 (16-17) ◽  
pp. 1409-1414 ◽  
Author(s):  
Anna Germanová ◽  
Alexandra Muravská ◽  
Marie Jáchymová ◽  
Zdeněk Hájek ◽  
Michal Koucký ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Gene Polymorphisms ◽  
Glyoxalase I ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Pathological Pregnancy ◽  
I Gene

The immunosuppressant FK506 inhibits amino acid import in Saccharomyces cerevisiae

1993 ◽  
Vol 13 (8) ◽  
pp. 5010-5019 ◽  
Author(s):  
J Heitman ◽  
A Koller ◽  
J Kunz ◽  
R Henriquez ◽  
A Schmidt ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Amino Acid ◽  
Cyclosporin A ◽  
Secretory Pathway ◽  
Yeast Cells ◽  
Amino Acid Transporters ◽  
Yeast Saccharomyces Cerevisiae ◽  
Eukaryotic Microorganisms

The immunosuppressants cyclosporin A, FK506, and rapamycin inhibit growth of unicellular eukaryotic microorganisms and also block activation of T lymphocytes from multicellular eukaryotes. In vitro, these compounds bind and inhibit two different types of peptidyl-prolyl cis-trans isomerases. Cyclosporin A binds cyclophilins, whereas FK506 and rapamycin bind FK506-binding proteins (FKBPs). Cyclophilins and FKBPs are ubiquitous, abundant, and targeted to multiple cellular compartments, and they may fold proteins in vivo. Previously, a 12-kDa cytoplasmic FKBP was shown to be only one of at least two FK506-sensitive targets in the yeast Saccharomyces cerevisiae. We find that a second FK506-sensitive target is required for amino acid import. Amino acid-auxotrophic yeast strains (trp1 his4 leu2) are FK506 sensitive, whereas prototrophic strains (TRP1 his4 leu2, trp1 HIS4 leu2, and trp1 his4 LEU2) are FK506 resistant. Amino acids added exogenously to the growth medium mitigate FK506 toxicity. FK506 induces GCN4 expression, which is normally induced by amino acid starvation. FK506 inhibits transport of tryptophan, histidine, and leucine into yeast cells. Lastly, several genes encoding proteins involved in amino acid import or biosynthesis confer FK506 resistance. These findings demonstrate that FK506 inhibits amino acid import in yeast cells, most likely by inhibiting amino acid transporters. Amino acid transporters are integral membrane proteins which import extracellular amino acids and constitute a protein family sharing 30 to 35% identity, including eight invariant prolines. Thus, the second FK506-sensitive target in yeast cells may be a proline isomerase that plays a role in folding amino acid transporters during transit through the secretory pathway.

Cloning and Characterization of a Glyoxalase I Gene from the Osmotolerant Yeast Candida magnoliae

2011 ◽  
Vol 21 (3) ◽  
pp. 277-283 ◽  
Author(s):  
Eun-Hee Park ◽  
Dae-Hee Lee ◽  
Jin-Ho Seo ◽  
Myoung-Dong Kim
Keyword(s):  
Glyoxalase I ◽  
Candida Magnoliae ◽  
I Gene ◽  
Osmotolerant Yeast

scholarly journals Preliminary Characterization of a Ni2+-Activated and Mycothiol-Dependent Glyoxalase I Enzyme from Streptomyces coelicolor

Inorganics ◽  
2019 ◽  
Vol 7 (8) ◽  
pp. 99 ◽  
Author(s):  
Uthaiwan Suttisansanee ◽  
John F. Honek
Keyword(s):  
Leishmania Major ◽  
Homo Sapiens ◽  
Streptomyces Coelicolor ◽  
Glyoxalase I ◽  
Glyoxalase System ◽  
Genetic Studies ◽  
Preliminary Characterization ◽  
Glyoxalase Ii ◽  
Activation Profile

The glyoxalase system consists of two enzymes, glyoxalase I (Glo1) and glyoxalase II (Glo2), and converts a hemithioacetal substrate formed between a cytotoxic alpha-ketoaldehyde, such as methylglyoxal (MG), and an intracellular thiol, such as glutathione, to a non-toxic alpha-hydroxy acid, such as d-lactate, and the regenerated thiol. Two classes of Glo1 have been identified. The first is a Zn2+-activated class and is exemplified by the Homo sapiens Glo1. The second class is a Ni2+-activated enzyme and is exemplified by the Escherichia coli Glo1. Glutathione is the intracellular thiol employed by Glo1 from both these sources. However, many organisms employ other intracellular thiols. These include trypanothione, bacillithiol, and mycothiol. The trypanothione-dependent Glo1 from Leishmania major has been shown to be Ni2+-activated. Genetic studies on Bacillus subtilis and Corynebacterium glutamicum focused on MG resistance have indicated the likely existence of Glo1 enzymes employing bacillithiol or mycothiol respectively, although no protein characterizations have been reported. The current investigation provides a preliminary characterization of an isolated mycothiol-dependent Glo1 from Streptomyces coelicolor. The enzyme has been determined to display a Ni2+-activation profile and indicates that Ni2+-activated Glo1 are indeed widespread in nature regardless of the intracellular thiol employed by an organism.

Glyoxalase I – structure, function and a critical role in the enzymatic defence against glycation

2003 ◽  
Vol 31 (6) ◽  
pp. 1343-1348 ◽  
Author(s):  
P.J. Thornalley
Keyword(s):  
Metal Ion ◽  
Catalytic Mechanism ◽  
Critical Role ◽  
Glyoxalase I ◽  
Water Molecules ◽  
Glyoxalase System ◽  
E Coli ◽  
Antimalarial Agents

Glyoxalase I is part of the glyoxalase system present in the cytosol of cells. The glyoxalase system catalyses the conversion of reactive, acyclic α-oxoaldehydes into the corresponding α-hydroxyacids. Glyoxalase I catalyses the isomerization of the hemithioacetal, formed spontaneously from α-oxoaldehyde and GSH, to S-2-hydroxyacylglutathione derivatives [RCOCH(OH)-SG→RCH(OH)CO-SG], and in so doing decreases the steady-state concentrations of physiological α-oxoaldehydes and associated glycation reactions. Physiological substrates of glyoxalase I are methylglyoxal, glyoxal and other acyclic α-oxoaldehydes. Human glyoxalase I is a dimeric Zn2+ metalloenzyme of molecular mass 42 kDa. Glyoxalase I from Escherichia coli is a Ni2+ metalloenzyme. The crystal structures of human and E. coli glyoxalase I have been determined to 1.7 and 1.5 Å resolution. The Zn2+ site comprises two structurally equivalent residues from each domain – Gln-33A, Glu-99A, His-126B, Glu-172B and two water molecules. The Ni2+ binding site comprises His-5A, Glu-56A, His-74B, Glu-122B and two water molecules. The catalytic reaction involves base-catalysed shielded-proton transfer from C-1 to C-2 of the hemithioacetal to form an ene-diol intermediate and rapid ketonization to the thioester product. R- and S-enantiomers of the hemithioacetal are bound in the active site, displacing the water molecules in the metal ion primary co-ordination shell. It has been proposed that Glu-172 is the catalytic base for the S-substrate enantiomer and Glu-99 the catalytic base for the R-substrate enantiomer; Glu-172 then reprotonates the ene-diol stereospecifically to form the R-2-hydroxyacylglutathione product. By analogy with the human enzyme, Glu-56 and Glu-122 may be the bases involved in the catalytic mechanism of E. coli glyoxalase I. The suppression of α-oxoaldehyde-mediated glycation by glyoxalase I is particularly important in diabetes and uraemia, where α-oxoaldehyde concentrations are increased. Decreased glyoxalase I activity in situ due to the aging process and oxidative stress results in increased glycation and tissue damage. Inhibition of glyoxalase I pharmacologically with specific inhibitors leads to the accumulation of α-oxoaldehydes to cytotoxic levels; cell-permeable glyoxalase I inhibitors are antitumour and antimalarial agents. Glyoxalase I has a critical role in the prevention of glycation reactions mediated by methylglyoxal, glyoxal and other α-oxoaldehydes in vivo.

Molecular cloning and characterization of a novel glyoxalase I gene TaGly I in wheat (Triticum aestivum L.)

2009 ◽  
Vol 37 (2) ◽  
pp. 729-735 ◽  
Author(s):  
Fanyun Lin ◽  
Jianhong Xu ◽  
Jianrong Shi ◽  
Hongwei Li ◽  
Bin Li
Keyword(s):  
Triticum Aestivum ◽  
Molecular Cloning ◽  
Triticum Aestivum L ◽  
Glyoxalase I ◽  
I Gene

scholarly journals Localization and Interaction of the Proteins Constituting the GAL Genetic Switch in Saccharomyces cerevisiae

2008 ◽  
Vol 7 (12) ◽  
pp. 2061-2068 ◽  
Author(s):  
Raymond Wightman ◽  
Rachel Bell ◽  
Richard J. Reece
Keyword(s):  
Gene Expression ◽  
Saccharomyces Cerevisiae ◽  
Cellular Localization ◽  
Transcriptional Control ◽  
Resonance Energy ◽  
Regulatory Proteins ◽  
Yeast Cells ◽  
Galactose Metabolism ◽  
Genetic Switch ◽  
Metabolism Regulation

ABSTRACT In Saccharomyces cerevisiae, the GAL genes encode the enzymes required for galactose metabolism. Regulation of these genes has served as the paradigm for eukaryotic transcriptional control over the last 50 years. The switch between inert and active gene expression is dependent upon three proteins—the transcriptional activator Gal4p, the inhibitor Gal80p, and the ligand sensor Gal3p. Here, we present a detailed spatial analysis of the three GAL regulatory proteins produced from their native genomic loci. Using a novel application of photobleaching, we demonstrate, for the first time, that the Gal3p ligand sensor enters the nucleus of yeast cells in the presence of galactose. Additionally, using Förster resonance energy transfer, we show that the interaction between Gal3p and Gal80p occurs throughout the yeast cell. Taken together, these data challenge existing models for the cellular localization of the regulatory proteins during the induction of GAL gene expression by galactose and suggest a mechanism for the induction of the GAL genes in which galactose-bound Gal3p moves from the cytoplasm to the nucleus to interact with the transcriptional inhibitor Gal80p.

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