Nucleotide sequence of the phosphoenolpyruvate carboxykinase gene from Saccharomyces cerevisiae

Stucka, Rolf; Valdes-Hevia, Marta D; Gancedo, Carlos; Schwarzlose, Christa; Feldmann, Heidi M.

doi:10.1093/nar/16.22.10926

Cited by 40 publications

(27 citation statements)

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“…These results allow us to conclude that the PCK 1 gene and not a suppressor has been cloned. Moreover, the sequence of the smallest insert [18] codes for a protein with an estimated molecular weight in accordance with the one reported for the PEPCK Fig.2. Southern-blot analysis of strains carrying a PCK 1 integrating plasmid or a disruption of the chromosomal PCK 1 gene.…”

Section: Resultssupporting

confidence: 80%

Isolation and characterization of the gene encoding phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae

1989

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The yeast PCKl gene codmg for phosphoenolpy~vate carboxykmasc (PEPCK) was Isolated by functIona complementatlon of pckl strains from S cerevzsfae Only one copy of the gene was found per baplold yeast gcnome An RNA of about 2 kb which hybndlzed with a DNA probe mtemal to the PCKl gene was found only m cells growmg m non-fermentable carbon sources Yeast &rams carrymg multiple copies of the PCKl gene showed normal catabohte represslon of PEPCK except those carrying the shortest msertlon complementmg the mutation (2 2 kb) that presented an altered kmetlcs of derepresslon Catabohte mactlvatlon was decreased m strains transfomed with multtcopy plasmlds carrymg the PCKl gene Phosphoenolpyruvate carboxykmase, Gluconeogenesls, Catabohte repression, Catabohte mactlvatlon

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Section: Resultssupporting

confidence: 80%

Isolation and characterization of the gene encoding phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae

1989

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“…Results of hydrophobicity analyses (10) were typical of a soluble protein. The amino acid sequence was 54% identical to the sequence of PEP carboxykinase from T. brucei (19) and 42% identical to the sequence of PEP carboxykinase from S. cerevisiae (24) when the sequences were aligned according to similarity of amino acid residues (20) (data not shown). One of the highly conserved regions contained the consensus for an ATP binding site (Fig.…”

Section: Resultsmentioning

confidence: 96%

Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae

et al. 1990

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The sequence of the pckA gene coding for phosphoenolpyruvate carboxykinase in Escherichia coli K-12 and previous molecular weight determinations indicate that this allosteric enzyme is a monomer of M, 51,316. The protein is homologous to ATP-dependent phosphoenolpyruvate carboxykinases from Trypanosoma brucei and Saccharomyces cerevisiwe. A potential ATP binding site was conserved in all three sequences. A potential binding site for the allosteric activator, calcium, identified in the E. coli enzyme, was only partially conserved in T. brucei and S. cerevisiae, consistent with the observation that the enzymes from the latter organisms were not activated by calcium. The published sequence of the ompR and envZ genes from Salmonella typhimurium is followed by a partial sequence that is highly homologous to pekA from E. coli. The order of these genes and the direction of transcription of the presumptive S. typhimurium pekA gene are the same as those in E. coli. The potential calcium binding site of the E. coil enzyme is conserved in the partial predicted sequence of the S. typhimurium phosphoenolpyruvate carboxykinase, consistent with the observation that calcium activation of the S. typhimurium phosphoenolpyruvase carboxykinase is very similar to that observed for the E. coli enzyme.

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“…The primary structure of ATP-dependent pckA genes from five organisms, Saccharomyces cerevisiae (46), Trypanosoma brucei (40), Trypanosoma cruzi (31), E. coli (35), and Rhizobium sp. strain NGR234 (39), have been characterized, and their encoded proteins were shown to share significant amino acid sequence similarity.…”

Section: Resultsmentioning

confidence: 99%

Molecular and expression analysis of the Rhizobium meliloti phosphoenolpyruvate carboxykinase (pckA) gene

1995

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The pckA gene of Rhizobium meliloti, encoding phosphoenolpyruvate carboxykinase, was isolated from a genomic cosmid library by complementation of the succinate growth phenotype of a Pck ؊ mutant. The gene region was mapped by subcloning and Tn5 insertion mutagenesis. The DNA sequence for a 2-kb region containing the structural gene and its promoter was determined. The pckA gene encodes a 536-amino-acid protein that shows homology with other ATP-dependent Pck enzymes. The promoter was identified following primer extension analysis and is similar to 70 -like promoters. Expression analysis with a pckA::lacZ gene fusion indicated that the pckA gene was strongly induced at the onset of stationary phase in complex medium. When defined carbon sources were tested, the expression level of the pckA gene was found to be high when cells were grown in minimal media with succinate or arabinose as the sole carbon source but almost absent when glucose, sucrose, or glycerol was the sole carbon source. Glucose and sucrose were not found to strongly repress pckA induction by succinate.Phosphoenolpyruvate carboxykinase (EC 4.1.1.49) (Pck) catalyzes the decarboxylation and phosphorylation of oxaloacetate to phosphoenolpyruvate. This reaction is the first step in the gluconeogenic pathway in which tricarboxylic acid (TCA) cycle intermediates are converted to hexose sugars. With the exceptions of phosphoenolpyruvate carboxykinase and fructose bisphosphatase, all of the enzymes employed in the gluconeogenic pathway are also used in the glycolytic pathway.With N 2 -fixing root nodules induced by bacteria such as the alfalfa symbiont Rhizobium meliloti, there is much evidence to suggest that the plant supplies the C 4 -dicarboxylic acids succinate and malate to the N 2 -fixing bacteria (bacteroids) within nodules (5,9,17,42,47,51). Pck is required for growth and metabolism of C 4 -dicarboxylates and other TCA cycle intermediates in free-living cells of R. meliloti, Rhizobium leguminosarum, and Rhizobium sp. strain NGR234. The symbiotic importance of Pck during nodule infection and N 2 fixation requires clarification. While Pck Ϫ mutants of R. meliloti show a reduced level of nitrogen fixation, Pck activity is not detected in wild-type bacteroids (15). R. leguminosarum Pck Ϫ mutants have no apparent symbiotic phenotype, yet Pck activity was detected at low levels in wild-type bacteroids (33). A Pck Ϫ mutant of Rhizobium sp. strain NGR234, a broad-host-range fast-growing rhizobium, exhibited a host-dependent symbiotic phenotype. N 2 fixation was reduced to 60 and 20% of the wild-type level in Leucaena leucocephala and Macroptilium atropurpureum, respectively, whereas on Vigna unguiculata, this mutant induced completely Fix Ϫ nodules (39). The structural analysis of these nodules showed defects in the nodule development process and the occurrence of early senescence of bacteroids. These results suggest that the importance of Pck in symbiosis is dependent on the plant host metabolites available to the bacteria during the infection process an...

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Nucleotide sequence of the phosphoenolpyruvate carboxykinase gene from Saccharomyces cerevisiae

Cited by 40 publications

References 1 publication

Isolation and characterization of the gene encoding phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae

Isolation and characterization of the gene encoding phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae

Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae

Molecular and expression analysis of the Rhizobium meliloti phosphoenolpyruvate carboxykinase (pckA) gene

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