Phosphoprotein with Phosphoglycerate Mutase Activity from the Archaeon
            <i>Sulfolobus solfataricus</i>

Potters, Mark; Solow, Barbara T.; Bischoff, Kenneth M.; Graham, David E.; Lower, Brian H.; Helm, Richard F.; Kennelly, Peter J.

doi:10.1128/jb.185.7.2112-2121.2003

Cited by 24 publications

(20 citation statements)

References 47 publications

(45 reference statements)

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“…tomato and B. phymatum STM815 (this study) to be an obligate enzyme for both glycolysis and gluconeogenesis. dPGM enzymes have previously been identified in some bacteria, such as Haemophilus influenzae (Fleischmann et al, 1995), Streptomyces coelicolor (White et al, 1992) and Zymomonas mobilis (Yomano et al, 1993), whereas only the iPGM enzymes are found in archaea (Graham et al, 2002;Potters et al, 2003). Surprisingly, both dPGM and iPGM are also found in some bacteria, such as E. coli and Bacillus subtilis, although only one form is predominantly active (Fraser et al, 1999;Watabe & Freese, 1979).…”

Section: Discussionmentioning

confidence: 99%

Effect of phosphoglycerate mutase and fructose 1,6-bisphosphatase deficiency on symbiotic Burkholderia phymatum

et al. 2012

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Burkholderia phymatum STM815 is a b-rhizobial strain that can effectively nodulate several species of the large legume genus Mimosa. Two Tn5-induced mutants of this strain, KM16-22 and KM51, failed to form root nodules on Mimosa pudica, but still caused root hair deformation, which is one of the early steps of rhizobial infection. Both mutants grew well in a complex medium. However, KM16-22 could not grow on minimal medium unless a sugar and a metabolic intermediate such as pyruvate were provided, and KM51 also could not grow on minimal medium unless a sugar was added. The Tn5-interrupted genes of the mutants showed strong homologies to pgm, which encodes 2,3-biphosphoglycerate-dependent phosphoglycerate mutase (dPGM), and fbp, which encodes fructose 1,6-bisphosphatase (FBPase). Both enzymes are known to be involved in obligate steps in carbohydrate metabolism. Enzyme assays confirmed that KM16-22 and KM51 had indeed lost dPGM and FBPase activity, respectively, whilst the activities of these enzymes were expressed normally in both free-living bacteria and symbiotic bacteroids of the parental strain STM815. Both mutants recovered their enzyme activity after the introduction of wild-type pgm or fbp genes, were subsequently able to use carbohydrate as a carbon source, and were able to form root nodules on M. pudica and to fix nitrogen as efficiently as the parental strain. We conclude that the enzymes dPGM and FBPase are essential for the formation of a symbiosis with the host plant.

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Section: Discussionmentioning

confidence: 99%

Effect of phosphoglycerate mutase and fructose 1,6-bisphosphatase deficiency on symbiotic Burkholderia phymatum

et al. 2012

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“…In our experience, it is not uncommon that only a portion of the peaks in the mass spectrum derived from an in situ tryptic digestion of what appeared to be a single polypeptide spot or band from an electrophoretic gel can be traced to a single ORF (43). The extreme sensitivity of contemporary mass spectrometers renders them capable of detecting peptides from other, relatively minor species that might be present in the section of gel that was analyzed.…”

Section: Vol 186 2004mentioning

confidence: 99%

A Phosphoprotein from the Archaeon Sulfolobus solfataricus with Protein-Serine/Threonine Kinase Activity

2004

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Sulfolobus solfataricus contains a membrane-associated protein kinase activity that displays a strong preference for threonine as the phospho-acceptor amino acid residue. When a partially purified detergent extract of the membrane fraction from the archaeon S. solfataricus that had been enriched for this activity was incubated with [␥-32 P]ATP, radiolabeled phosphate was incorporated into roughly a dozen polypeptides, several of which contained phosphothreonine. One of the phosphothreonine-containing proteins was identified by mass peptide profiling as the product of open reading frame [ORF] sso0469. Inspection of the DNA-derived amino acid sequence of the predicted protein product of ORF sso0469 revealed the presence of sequence characteristics faintly reminiscent of the "eukaryotic" protein kinase superfamily. ORF sso0469 therefore was cloned, and its polypeptide product was expressed in Escherichia coli. The recombinant protein formed insoluble aggregates that could be dispersed using urea or detergents. The solubilized polypeptide phosphorylated several exogenous proteins in vitro, including casein, myelin basic protein, and bovine serum albumin. Mutagenic alteration of amino acids predicted to be essential for catalytic activity abolished or severely reduced catalytic activity. Phosphorylation of exogenous substrates took place on serine and, occasionally, threonine. This new archaeal protein kinase displayed no catalytic activity when GTP was substituted for ATP as the phospho-donor substrate, while Mn 2؉ was the preferred cofactor.The versatility of covalent phosphorylation-dephosphorylation as a mechanism for regulating protein function and transducing extracellular signals has been compellingly demonstrated in numerous studies encompassing a broad spectrum of eucaryal and bacterial organisms (reviewed in references 5, 15, 19, 22, 23, and 28). However, while protein phosphorylation has been detected in several members of the third phylogenetic domain, the Archaea (24,41,50,51,53,54,56,57), we know relatively little concerning the chemical nature, enzymatic catalysts, and physiological roles of archaeal protein phosphorylation-dephosphorylation events (reviewed in reference 27). Only a few archaeal proteins have been implicated as the targets of protein phosphorylation to date. They include a CheY homolog in Halobacterium salinarium (45), a methyltransferase-activating protein from Methanosarcina barkeri (11), an aminopeptidase from Sulfolobus solfataricus (9), and a glycogen synthase from Sulfolobus acidocaldarius (7). In addition, the N-terminal sequences of three phosphotyrosine-containing proteins from Thermococcus kodakaraensis KOD1 have been determined, although the full sequences of these phosphoproteins have yet to be identified (24 (26,27,32,42,49). However, in only a few instances have the inferences of these in silico analyses been translated into the direct, empirical identification and characterization of defined gene products displaying the predicted functional capabilities. Included among ...

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“…This proposed mechanism is in agreement with the finding that the characterized iPGAM from Sul. solfataricus autophosphorylates at this conserved serine residue (215).…”

Section: Phosphoglycerate Kinasementioning

confidence: 99%

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

Bräsen

Esser

Rauch

et al. 2014

Microbiol Mol Biol Rev

279

294

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SUMMARY The metabolism of Archaea , the third domain of life, resembles in its complexity those of Bacteria and lower Eukarya . However, this metabolic complexity in Archaea is accompanied by the absence of many “classical” pathways, particularly in central carbohydrate metabolism. Instead, Archaea are characterized by the presence of unique, modified variants of classical pathways such as the Embden-Meyerhof-Parnas (EMP) pathway and the Entner-Doudoroff (ED) pathway. The pentose phosphate pathway is only partly present (if at all), and pentose degradation also significantly differs from that known for bacterial model organisms. These modifications are accompanied by the invention of “new,” unusual enzymes which cause fundamental consequences for the underlying regulatory principles, and classical allosteric regulation sites well established in Bacteria and Eukarya are lost. The aim of this review is to present the current understanding of central carbohydrate metabolic pathways and their regulation in Archaea . In order to give an overview of their complexity, pathway modifications are discussed with respect to unusual archaeal biocatalysts, their structural and mechanistic characteristics, and their regulatory properties in comparison to their classic counterparts from Bacteria and Eukarya . Furthermore, an overview focusing on hexose metabolic, i.e., glycolytic as well as gluconeogenic, pathways identified in archaeal model organisms is given. Their energy gain is discussed, and new insights into different levels of regulation that have been observed so far, including the transcript and protein levels (e.g., gene regulation, known transcription regulators, and posttranslational modification via reversible protein phosphorylation), are presented.

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Phosphoprotein with Phosphoglycerate Mutase Activity from the Archaeon Sulfolobus solfataricus

Cited by 24 publications

References 47 publications

Effect of phosphoglycerate mutase and fructose 1,6-bisphosphatase deficiency on symbiotic Burkholderia phymatum

Effect of phosphoglycerate mutase and fructose 1,6-bisphosphatase deficiency on symbiotic Burkholderia phymatum

A Phosphoprotein from the Archaeon Sulfolobus solfataricus with Protein-Serine/Threonine Kinase Activity

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

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