The gene encoding glyoxalase I from Pseudomonas putida: cloning, overexpression, and sequence comparisons with human glyoxalase I

Lu, Tianfen; Creighton, Donald J.; Antoine, Miquel D.; Fenselau, Catherine; Lovett, Paul S.

doi:10.1016/0378-1119(94)90864-8

Cited by 22 publications

(20 citation statements)

References 12 publications

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“…In parallel, the gloA gene was cloned under its own promoter into plasmid pHG165 (Stewart et al ., 1986), creating pMJM1, to achieve limited overexpression of the protein. We also obtained the Pseudomonas putida glyoxalase gene ( glxI ) cloned in the high‐expression plasmid pBTac1 (Lu et al ., 1994). Glyoxalase I activity was assayed in extracts prepared from mid‐log phase cells grown in minimal media using the Δ gloA strain, MJF388, the wild‐type MJF274, MJF274/pBTac1/ glxI and from MJF274/pMJM1.…”

Section: Resultsmentioning

confidence: 99%

The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K⁺ efflux system in Escherichia coli

MacLean

Ness

Ferguson

et al. 1998

Molecular Microbiology

115

141

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SummaryThe glyoxalase I gene (gloA) of Escherichia coli has been cloned and used to create a null mutant. Cells overexpressing glyoxalase I exhibit enhanced tolerance of methylglyoxal (MG) and exhibit elevated rates of detoxification, although the increase is not stoichiometric with the change in enzyme activity. Potassium efflux via KefB is also enhanced in the overexpressing strain. Analysis of the physiology of the mutant has revealed that growth and viability are quite normal, unless the cell is challenged with MG either added exogenously or synthesized by the cells. The mutant strain has a low rate of detoxification of MG, and cells rapidly lose viability when exposed to this electrophile. Activation of KefB and KefC is diminished in the absence of functional glyoxalase I. These data suggest that the glutathione-dependent glyoxalase I is the dominant detoxification pathway for MG in E. coli and that the product of glyoxalase I activity, S-lactoylglutathione, is the activator of KefB and KefC.

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Section: Resultsmentioning

confidence: 99%

The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K⁺ efflux system in Escherichia coli

MacLean

Ness

Ferguson

et al. 1998

Molecular Microbiology

115

141

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“…Two other potential ATG codons in the samereading frame located at positions + 120 and + 177 fitted poorly that consensus. The putative protein encoded by the longest ORF was 185 amino acids long (molecular mass 20.7 kDa, pI 5.16) and showed extensive sequence similarity to glyoxalase-I from Pseudomonasputida [ 13] and human colon [20] (Fig. 2).…”

Section: Isolation and Characterization Of Glyoxalase-i Cdnamentioning

confidence: 99%

Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress

1995

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A cDNA, GLX1, encoding glyoxalase-I was isolated by differential screening of salt-induced genes in tomato. Glyoxalases-I and -II are ubiquitous enzymes whose functions are not clearly understood. They may serve to detoxify methylglyoxal produced from triosephosphates in all cells. The protein encoded by GLX1 shared 49.4% and 58.5% identity with glyoxalase-I isolated from bacteria and human, respectively. Furthermore, yeast cells expressing GLX1 showed a glyoxalase-I specific activity 20-fold higher than non-transformed cells. Both GLX1 mRNA and glyoxalase-I polypeptide levels increased 2- to 3-fold in roots, stems and leaves of plants treated with either NaCl, mannitol, or abscisic acid. Immunohistochemical localization indicated that glyoxalase-I was expressed in all cell types, with preferential accumulation in phloem sieve elements. This expression pattern was not appreciably altered by salt-stress. We suggest that the increased expression of glyoxalase-I may be linked to a higher demand for ATP generation and to enhanced glycolysis in salt-stressed plants.

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“…This is the second case in which the evolutionary relationship among the GlxI sequences is not as predicted. Pseudomonas putida, although a bacterial organism, has a higher sequence similarity to eukaryotes (Lu et al 1994;Clugston et al 1997). Although the two new plant sequences appear to be most similar to the yeast in terms of their overall structural relationship, as fused dimers, they segregate more closely to the bacterial sequences, based purely on amino acid sequence comparisons of their N-and C-terminal halves.…”

Section: Resultsmentioning

confidence: 99%

“…The sequences of several GlxI enzymes have been reported (Inoue and Kimura 1996;Lu et al 1994;Espartero et al 1995;Kim et al 1993;Ranganathan et al 1993;Ridderström and Mannervik 1996a;Clugston et al 1997). Previously, a comparison was made between the sequences of enzymes known to have GlxI activity and several open reading frames with unassigned function that had significant homology to known GlxI enzymes (Clugston et al 1997).…”

Section: Introductionmentioning

confidence: 99%

Identification of Glyoxalase I Sequences in Brassica oleracea and Sporobolus stapfianus: Evidence for Gene Duplication Events

1998

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Glyoxalase I (GlxI) is the first of two enzymes involved in the cellular detoxification of methylglyoxal. A recent search of the National Center for Biotechnology Information (NCBI) databases with the protein sequence of Salmonella typhimurium GlxI identified two new hypothetical proteins with unassigned function. These two sequences, from Brassica oleracea and Sporobolus stapfianus, have significant sequence similarity to known GlxI sequences, suggesting that these two open reading frames encode for GlxI in these plants. Interestingly, analysis of these two new sequences indicates that they code for a protein composed of two fused monomers, a situation previously found solely in the yeast GlxI enzymes.

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The gene encoding glyoxalase I from Pseudomonas putida: cloning, overexpression, and sequence comparisons with human glyoxalase I

Cited by 22 publications

References 12 publications

The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K⁺ efflux system in Escherichia coli

The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K⁺ efflux system in Escherichia coli

Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress

Identification of Glyoxalase I Sequences in Brassica oleracea and Sporobolus stapfianus: Evidence for Gene Duplication Events

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The gene encoding glyoxalase I from Pseudomonas putida: cloning, overexpression, and sequence comparisons with human glyoxalase I

Cited by 22 publications

References 12 publications

The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli

The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli

Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress

Identification of Glyoxalase I Sequences in Brassica oleracea and Sporobolus stapfianus: Evidence for Gene Duplication Events

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The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K⁺ efflux system in Escherichia coli

The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K⁺ efflux system in Escherichia coli