Adaptive response of the archaeon Sulfolobus acidocaldarius BC65 to phosphate starvation

Osorío, Gonzalo; Jerez, Carlos A.

doi:10.1099/13500872-142-6-1531

Cited by 30 publications

(24 citation statements)

References 32 publications

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“…Growth of Sulfolobus acidocaldarius in the presence of radiolabeled phosphate under limited-phosphate conditions revealed the existence of numerous phosphoproteins (319). In particular, the phosphorylation of a 36-kDa protein was augmented under phosphate starvation, hinting at a regulatory role in a cellular response pathway for this protein.…”

Section: Targets and Functions Of Protein Phosphorylation In Archaeamentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

196

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One of the first hurdles to be negotiated in the postgenomic era involves the description of the entire protein content of the cell, the proteome. Such efforts are presently complicated by the various posttranslational modifications that proteins can experience, including glycosylation, lipid attachment, phosphorylation, methylation, disulfide bond formation, and proteolytic cleavage. Whereas these and other posttranslational protein modifications have been well characterized in Eucarya and Bacteria, posttranslational modification in Archaea has received far less attention. Although archaeal proteins can undergo posttranslational modifications reminiscent of what their eucaryal and bacterial counterparts experience, examination of archaeal posttranslational modification often reveals aspects not previously observed in the other two domains of life. In some cases, posttranslational modification allows a protein to survive the extreme conditions often encountered by Archaea. The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by posttranslational modification in Archaea form the focus of this review

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Section: Targets and Functions Of Protein Phosphorylation In Archaeamentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

196

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“…Phosphorylated proteins have been detected in several halophilic, methanogenic, and thermophilic archaeons (11,26,48,62,63,65,66,68,69), and in several cases the observed patterns of protein phosphorylation exhibited the type of environmentally sensitive changes suggestive of regulatory control (48,62,68,69). A CheA-like two-component cascade responsible for modulating chemo-and phototaxis has been characterized for the halophilic archaeon Halobacterium halobium (52,53), while protein-serine/threonine phosphatases belonging to the PPP family of enzymes first discovered in the Eucarya have been described for the archaeons Sulfolobus solfataricus (32,37), Methanosarcina thermophila TM-1 (49,67), and Pyrodictium abyssi TAG11 (41).…”

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Open Reading Frame sso2387 from the Archaeon Sulfolobus solfataricus Encodes a Polypeptide with Protein-Serine Kinase Activity

Lower

Kennelly

2003

J Bacteriol

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The predicted polypeptide product of open reading frame sso2387 from the archaeon Sulfolobus solfataricus, SsoPK2, displayed several of the sequence features conserved among the members of the "eukaryotic" protein kinase superfamily. sso2387 was cloned, and its polypeptide product was expressed in Escherichia coli. The recombinant protein, rSsoPK2, was recovered in insoluble aggregates that could be dispersed by using high concentrations (5 M) of urea. The solubilized polypeptide displayed the ability to phosphorylate itself as well as several exogenous proteins, including mixed histones, casein, bovine serum albumin, and reduced carboxyamidomethylated and maleylated lysozyme, on serine residues. The source of this activity resided in that portion of the protein displaying homology to the catalytic domain of eukaryotic protein kinases. By use of mass spectrometry, the sites of autophosphorylation were found to be located in two areas, one immediately N terminal to the region corresponding to subdomain I of eukaryotic protein kinases, and the second N terminal to the presumed activation loop located between subdomains VII and VIII. Autophosphorylation of rSsoPK2 could be uncoupled from the phosphorylation of exogenous proteins by manipulation of the temperature or mutagenic alteration of the enzyme. Autophosphorylation was detected only at temperatures >60°C, whereas phosphorylation of exogenous proteins was detectable at 37°C. Similarly, replacement of one of the potential sites of autophosphorylation, Ser 548 , with alanine blocked autophosphorylation but not phosphorylation of an exogenous protein, casein.The reversible alteration of the functional properties of strategically selected proteins by phosphorylation-dephosphorylation represents one of nature's most widely employed means for controlling cellular processes (reviewed in reference 30). The scientific literature provides numerous examples of the prominent role played by this versatile regulatory mechanism in members of the Eucarya (reviewed in references 17, 18, and 24) and the Bacteria (reviewed in references 2, 7, and 22). By contrast, we know very little concerning the chemical nature, enzymatic catalysts, or physiological roles of the protein phosphorylation-dephosphorylation events that take place in members of the so-called third domain of life, the Archaea. Such knowledge is important not only for understanding how these biologically diverse organisms adapt to the extreme environments in which they typically reside but also for tracing the origins and evolution of a fundamentally important regulatory mechanism.The available evidence suggests that protein phosphorylation is a fairly general phenomenon among the Archaea. Phosphorylated proteins have been detected in several halophilic, methanogenic, and thermophilic archaeons (11,26,48,62,63,65,66,68,69), and in several cases the observed patterns of protein phosphorylation exhibited the type of environmentally sensitive changes suggestive of regulatory control (48,62,68,69). A CheA-like two-compo...

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“…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.…”

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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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Adaptive response of the archaeon Sulfolobus acidocaldarius BC65 to phosphate starvation

Cited by 30 publications

References 32 publications

Posttranslational Protein Modification inArchaea

Posttranslational Protein Modification inArchaea

Open Reading Frame sso2387 from the Archaeon Sulfolobus solfataricus Encodes a Polypeptide with Protein-Serine Kinase Activity

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

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