Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus

Schläpfer, Beatrice S.; Zuber, Herbert

doi:10.1016/0378-1119(92)90031-j

Cited by 36 publications

(24 citation statements)

References 44 publications

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“…Previous work with B. megaterium has indicated that the gap, pgk, and tpi genes are clustered on the chromosome with an additional unidentified ORF just upstream ofgap and a second ORF, which we have now shown ispgm, just downstream of tpi (15). This same cluster of genes encoding glycolytic enzymes seems likely to be present in B. subtilis as well and includes eno just downstream of pgm.…”

Section: Discussionsupporting

confidence: 65%

“…However, the small (or no) intergenic space between pgk, tpi, pgm, and eno suggests that these genes are likely to be cotranscribed. In B. megaterium there is a 312-bp gap between the end of gap and t-he beginning of pgk (15), and this gap is at least 232 bp in B. subtilis (29). Although the presence of gap just upstream of pgk in B. subtilis has not yet been shown definitively, this certainly seems likely.…”

Section: Discussionmentioning

confidence: 98%

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Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis

Leyva‐Vázquez

Setlow

1994

J Bacteriol

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The Bacilus subtilis genes tpi, pgm, and eno, encoding triose phosphate isomerase, phosphoglycerate mutase (PGM), and enolase, respectively, have been cloned and sequenced. These genes are the last three in a large putative operon coding for glycolytic enzymes; the operon includes pgk (coding for phosphoglycerate kinase) followed by tpi, pgm, and eno. The triose phosphate isomerase and enolase from B. subtilis are extremely similar to those from all other species, both eukaryotic and prokaryotic. However, B. subtilis PGM bears no resemblance to mammalian, fungal, or gram-negative bacterial PGMs, which are dependent on 2,3-diphosphoglycerate (DPG) for activity. Instead, B. subtilis PGM, which is DPG independent, is very similar to a DPG-independent PGM from a plant species but differs from the latter in the absolute requirement of B. subtilis PGM for Mn2 . The cloned pgm gene has been used to direct up to 25-fold overexpression of PGM in Escherichia coli; this should facilitate purification of large amounts of this novel Mn2'-dependent enzyme.Inactivation ofpgm plus eno in B. subtilis resuIted in extremely slow growth either on plates or in liquid, but growth of these mutants was enhanced by supplementation of media with malate. However, these mutants were asporogenous with or without malate supplementation.The process of sporulation in Bacillus and Clostridium species produces a spore which is extremely resistant to a variety of harsh treatments, such as heat, dessication and radiation, and which can survive for long periods in the absence of exogenous nutrients (19). One reason for the survival of spores in such conditions is that they are metabolically dormant and carry out neither macromolecular biosynthesis nor detectable metabolism of exogenous or endogenous compounds (17-19). Not surprisingly, dormant spores lack significant levels of products of catabolism such as ATP and NADH, which are present at high levels in growing cells, although AMP and NAD are present at significant levels in spores (18). While the spore can remain in this dormant state for long periods of time, with the proper stimulus spore germination is initiated, and within minutes ATP and NADH are produced and macromolecular biosynthesis begins (17, 18). The dormant spore contains a number of energy reserves which are mobilized in the first minutes of germination, thus facilitating the rapid resumption of metabolism. One such reserve is the large depot of small, acid-soluble proteins which are degraded to amino acids early in germination, with a significant amount of these amino acids catabolized for energy (17,18). A second energy reserve is a depot of 3-phosphoglyceric acid (3PGA), which constitutes 0.2 to 0.5% of spore dry weight (18). The 3PGA depot is accumulated late in sporulation within the developing spore, and there is a body of evidence indicating that phosphoglycerate mutase (PGM) is the enzyme which is specifically inhibited to allow 3PGA accumulation (18,20,22). In the first minutes of germination, the 3PGA depot is converted ...

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Section: Discussionsupporting

confidence: 65%

Section: Discussionmentioning

confidence: 98%

Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis

Leyva‐Vázquez

Setlow

1994

J Bacteriol

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“…Evidence for glycolytic enzyme gene operons include linked pyruvate kinase and PFK genes in Clostridium acetobutylicum (Belouski et al, 1998); clustered genes for phosphoglycerate kinase (PGK), triosephosphate isomerase (TPI), phosphoglycerate mutase and enolase in Baccilus subtilis (Leyva-Vazquez and Setlow, 1994); linkage of GAPDH, PGK and TPI in Borrelia megaterium, Borrelia bungorferi and Borrelia hermsii (Gebbia et al, 1997;Schlapfer and Zuber, 1992); clustering of fructose 1,6-biphosphate aldolase, 3-phosphoglycerate kinase and GAPDH in E. coli (Alefounder and Perham 1989), and clustering of the glucose-6 dehydrogenase, 6-phosphogluconate dehydratase and glucokinase genes with a putative glucose transporter in Zymomonas mobilis (Barnell et al, 1990). These glycolytic enzyme gene operons may be regulated independently of each other or globally.…”

Section: Substrate Regulation By Operons In Bacteriamentioning

confidence: 99%

Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia

Webster

2003

Journal of Experimental Biology

149

107

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SUMMARYTwo billion years of aerobic evolution have resulted in mammalian cells and tissues that are extremely oxygen-dependent. Exposure to oxygen tensions outside the relatively narrow physiological range results in cellular stress and toxicity. Consequently, hypoxia features prominently in many human diseases, particularly those associated with blood and vascular disorders,including all forms of anemia and ischemia. Bioenergetic enzymes have evolved both acute and chronic oxygen sensing mechanisms to buffer changes of oxygen tension; at normal PO oxidative phosphorylation is the principal energy supply for eukaryotic cells, but when the PO falls below a critical mark metabolic switches turn off mitochondrial electron transport and activate anaerobic glycolysis. Without this switch cells would suffer an immediate energy deficit and death at low PO. An intriguing feature of the switching is that the same conditions that regulate energy metabolism also regulate bioenergetic genes, so that enzyme activity and transcription are regulated simultaneously,albeit with different time courses and signaling pathways. In this review we explore the pathways mediating hypoxia-regulated glycolytic enzyme gene expression, focusing on their atavistic traits and evolution.

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“…The gapDH gene encodes glyceraldehyde-3-phosphate dehydrogenase (GapDH), an essential component of glycolysis (Prescott et al, 1993). The gapDH locus has been used to describe the taxonomic positions of several taxa at the species level (Lawrence et al, 1991 ;Schlaeper & Zuber, 1992 ;Liaud et al, 1994). Phylogenetic utility of this gene has been attributed to the unusually slow third position substitution rate observed among gapDH codons (Lawrence et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Phylogenetic relationships of necrogenic Erwinia and Brenneria species as revealed by glyceraldehyde-3-phosphate dehydrogenase gene sequences.

Brown¹,

Davis²,

Gouk³

et al. 2000

International Journal of Systematic and Evolutionary Microbiology

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Recent examination of the relationships of the dry necrosis-inducing (necrogenic) erwinias using 16S rDNA sequences demonstrated that these bacteria comprise a polyphyletic group and, therefore, have been subdivided into three distinct genera, Erwinia, Brenneria and Pectobacterium, with the classical ' amylovora ' group species now being distributed nearly evenly among the first two. To further assess the molecular evolutionary relationships between current necrogenic Erwinia and Brenneria species, as well as between these genera and the exclusively soft-rotting genus Pectobacterium, the glyceraldehyde-3-phosphate dehydrogenase (gapDH) genes from 57 Erwinia and Brenneria isolates along with Pectobacterium type strains were PCRamplified, sequenced and subjected to phylogenetic analysis. Pairwise alignments of cloned gapDH genes revealed remarkably high interspecies genetic diversity among necrogenic isolates. Four evolutionary clades of necrogenic species were described that assorted more closely to known softrotting species than to each other. Interclade comparisons of gapDH nucleotide sequences revealed as much genetic divergence between these four necrogenic clades as existed between necrogenic and soft-rotting clades. An examination of the phylogenetic utility of the gapDH gene in light of current 16S rDNA clustering of these species revealed varying levels of taxonomic congruence between these genes for the structure of Erwinia, Brenneria and Pectobacterium. These analyses suggest that, while gapDH possesses sufficient genetic variation to fully differentiate Erwinia and Brenneria species, the gene may not accurately reflect interspecies taxonomic relatedness among all three phytopathogenic genera.

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Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus

Cited by 36 publications

References 44 publications

Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis

Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis

Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia

Phylogenetic relationships of necrogenic Erwinia and Brenneria species as revealed by glyceraldehyde-3-phosphate dehydrogenase gene sequences.

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