Multiple Levels of Regulation ofEscherichia coliSuccinyl-CoA Synthetase

Birney, M; Um, Hong‐Duck; Klein, Claudette

doi:10.1006/abbi.1997.0313

Cited by 4 publications

(4 citation statements)

References 25 publications

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“…A functionally active succinyl-CoA ligase complex consists of two subunits, namely Lsc1p and Lsc2p. 55,56 The observation that Lsc1p shows an intermediary half-life of only 11 h is a further illustration that, apparently, proteins active within a single functional complex can show different protein dynamics.…”

Section: The Central Carbon Metabolismmentioning

confidence: 98%

The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in Saccharomyces cerevisiae

et al. 2011

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To establish more advanced models of molecular dynamics within cells, protein characteristics such as turnover rate and absolute instead of relative abundance have to be analyzed. We applied a proteomics strategy to analyze protein degradation and abundance in Saccharomyces cerevisiae. We used steady-state chemostat cultures to ascertain well-defined growth conditions and nitrogen limited media, which allowed us to rapidly switch from (14)N to (15)N-isotope containing media and to monitor the decay of the (14)N mono-isotope signals in time. We acquired both protein abundance information and degradation rates of 641 proteins. Half-lives of individual proteins were very diverse under nitrogen-limited steady-state conditions, ranging from less than 30 min to over 20 h. Proteins that act as single physical complexes do not always show alike half-lives. For example the chaperonin-containing TCP-1 complex showed similar intermediate half-lives ranging from 7 to 20 h. In contrast, the ribosome exhibited a wide diversity of half-lives ranging from 2.5 to over 20 h, although their cellular abundances were rather similar. The stabilities of proteins involved in the central sugar metabolism were found to be intermediary, except for the glycolytic enzymes Hxk1p and Fba1p and the TCA-cycle proteins Lsc2p and Kgd1p, which showed half-lives of over 20 h. These data stress the need for inclusion of quantitative data of protein turn-over rates in yeast systems biology.

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Section: The Central Carbon Metabolismmentioning

confidence: 98%

The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in Saccharomyces cerevisiae

et al. 2011

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“…It appears that the GTP modulates the amount of an inhibitor protein that controls the phosphorylation of the enzyme. The inhibitor E. coli protein also recognizes eukaryotic forms of succinyl-CoA ligase [15]. Based on these observations, it was proposed that succinyl-CoA ligase is a fourth control point in the TCA cycle [15].…”

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confidence: 99%

“…The inhibitor E. coli protein also recognizes eukaryotic forms of succinyl-CoA ligase [15]. Based on these observations, it was proposed that succinyl-CoA ligase is a fourth control point in the TCA cycle [15]. Other studies have uncovered additional levels of regulation on succinyl-CoA ligase function.…”

mentioning

confidence: 99%

Genes of succinyl‐CoA ligase from Saccharomyces cerevisiae

Przybyla-Zawislak

Dennis

Zakharkin

et al. 1998

European Journal of Biochemistry

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Succinyl-CoA ligase (succinyl-CoA synthetase) catalyzes the nucleotide-dependent conversion of succinyl-CoA to succinate. This enzyme functions in the tricarboxylic acid (TCA) cycle and is also involved in ketone-body breakdown in animals. The enzyme is composed of A and β subunits that are required for catalytic activity. Two genes, LSC1 (YOR142W) and LSC2 (YGR244C), with high similarity to succinylCoA ligase subunits from other species were isolated from Saccharomyces cerevisiae. The expression of these genes was repressed by growth on glucose and was induced threefold to sixfold during growth on nonfermentable carbon sources. The LSC genes were deleted singly and in combination. Unlike other yeast strains with defects in TCA cycle genes, strains lacking either or both LSC genes were able to grow with acetate as a carbon source. However, growth on glycerol or pyruvate was impaired. An antiserum against both subunits of the Escherichia coli enzyme was capable of recognizing the yeast succinyl-CoA ligase A subunit, and this band was absent in ∆lsc1 deletion strains. Succinyl-CoA ligase activity was absent in mitochondria isolated from strains deleted for one or both LSC genes, but activity was restored by the presence of the appropriate LSC gene on a plasmid. The yeast succinyl-CoA ligase was shown to utilize ATP but not GTP for succinyl-CoA synthesis.Keywords : succinyl-CoA ligase ; tricarboxylic acid cycle; mitochondria; Saccharomyces cerevisiae; yeast.Succinyl-CoA ligase (succinyl-CoA synthetase ; succinate thiokinase) catalyzes the nucleotide-dependent conversion of succinyl-CoA to succinate [1]. This is the only enzyme of the tricarboxylic acid (TCA) cycle that directly produces a highenergy phosphate. Succinyl-CoA ligase is composed of A and β subunits that function either as dimers or tetramers. The Escherichia coli enzyme is an A 2 β 2 tetramer, in which two independently active heterodimers are capable of synergistic interaction with the substrate [1Ϫ3]. The porcine heart mitochondrial enzyme has also been well characterized and, like other eukaryotic isoforms, it functions as an Aβ heterodimer [4]. In both prokaryotes and eukaryotes, the A subunit is phosphorylated on a conserved histidine residue, and the phosphate is subsequently transferred to form ATP or GTP [1]. Alteration of this residue by mutagenesis results in an inactive enzyme [5].Isoforms of succinyl-CoA ligase have been distinguished on the basis of their nucleotide preference for either GTP or ATP. The E. coli and Pseudomonas aeruginosa enzymes can utilize either ATP or GTP [1,6,7]. Eukaryotic succinyl-CoA ligases can be either ATP or GTP dependent [1]. While the ATP-dependent form is involved in TCA-cycle metabolism, the GTP-dependent form has been associated with ketone-body breakdown and heme biosynthesis [8,9]. The purified enzyme from Dichtyostelium discoideum shows specificity for GTP, while the enzyme Correspondence to M. T. McCammon,

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“…Two of the mutations (Q247R and W248R) occurred in sites known to modify the dimer–dimer interaction. The mutational profiles suggest that the gross catalytic activities of the SUCC–SUCD heterotetramer are not essentially modified, but that the fine-tuning allosteric control through substrate synergism, characteristic of this enzyme (Birney et al. 1997), might be modified.…”

Section: Discussionmentioning

confidence: 99%

Evolutionary Changes after Translational Challenges Imposed by Horizontal Gene Transfer

Bedhomme

Amorós-Moya

Valero

et al. 2019

Genome Biology and Evolution

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Genes acquired by horizontal gene transfer (HGT) may provide the recipient organism with potentially new functions, but proper expression level and integration of the transferred genes in the novel environment are not granted. Notably, transferred genes can differ from the receiving genome in codon usage preferences, leading to impaired translation and reduced functionality.Here, we characterize the genomic and proteomic changes undergone during experimental evolution of Escherichia coli after HGT of three synonymous versions, presenting very different codon usage preference, of an antibiotic resistance gene. The experimental evolution was conducted with and without the corresponding antibiotic and the mutational patterns and proteomic profiles after 1,000 generations largely depend on the experimental growth conditions (e.g., mutations in antibiotic off-target genes), and on the synonymous gene version transferred (e.g., mutations in genes responsive to translational stress). The transfer of an exogenous gene extensively modifies the whole proteome, and these proteomic changes are different for the different version of the transferred gene. Additionally, we identified conspicuous changes in global regulators and in intermediate metabolism, confirmed the evolutionary ratchet generated by mutations in DNA repair genes and highlighted the plasticity of bacterial genomes accumulating large and occasionally transient duplications.Our results support a central role of HGT in fuelling evolution as a powerful mechanism promoting rapid, often dramatic genotypic and phenotypic changes. The profound reshaping of the pre-existing geno/phenotype allows the recipient bacteria to explore new ways of functioning, far beyond the mere acquisition of a novel function.

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Multiple Levels of Regulation ofEscherichia coliSuccinyl-CoA Synthetase

Cited by 4 publications

References 25 publications

The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in Saccharomyces cerevisiae

The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in Saccharomyces cerevisiae

Genes of succinyl‐CoA ligase from Saccharomyces cerevisiae

Evolutionary Changes after Translational Challenges Imposed by Horizontal Gene Transfer

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