A Protein-Serine Phosphatase from the Halophilic Archaeon Haloferax volcanii

Oxenrider, Keith A.; Kennelly, Peter J.

doi:10.1006/bbrc.1993.1970

Cited by 21 publications

(20 citation statements)

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“…With respect to many of its functional properties, i.e. its stimulation by divalent metal ions, binding to and elution from hydroxylapatite and DE-52, apparent substrate affinity, and sensitivity to diethylpyrocarbonate, this enzyme strongly resembled the archaeal protein phosphatases that we had previously identified in the extreme acidothermophile, Sulfolobus solfataricus [lo], and the halophile, Haloferax volcanii [16]. Thus, it would appear that these enzymes are members of a common archaeal family of divalent metal ion-stimulated protein-serine/threonine phosphatases.…”

Section: Discussionmentioning

confidence: 74%

Inhibition of an archaeal protein phosphatase activity by okadaic acid, microcystin‐LR, or calyculin A

Oxenrider¹,

Rasche²,

Thorsteinsson³

et al. 1993

FEBS Letters

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Soluble extracts of the methanogenic archaeon, Methanosurcina thermophilu TM-l, contained a divalent metal ion-stimulated protein-serine phosphatase activity. This activity was sensitive to micromolar concentrations of okadaic acid, microcystin-LR, or calyculin A, three compounds thought to be highly specific inhibitors of the type 1/2A/2B genetic superfamily of eukaryotic protein-serine/threonine phosphatases. The observation that each of these three chemically unrelated compounds inhibited this archaeal protein phosphatase activity suggests the existence of structural homology, and perhaps even common genetic ancestry, with the type 1/2A/2B superfamily of protein-serine/threonine phosphatases found in eukaryotic organisms.Protein phosphatase; Okadaic acid; Microcystin-LR, Calyculin A, Archaea

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Section: Discussionmentioning

confidence: 74%

Inhibition of an archaeal protein phosphatase activity by okadaic acid, microcystin‐LR, or calyculin A

Oxenrider¹,

Rasche²,

Thorsteinsson³

et al. 1993

FEBS Letters

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“…In contrast, the three archaeal PPP family members require the addition of metal ions such as Mn 2ϩ for activity, as is the case for bacterial PPP family protein serine/threonine phosphatases (391). Finally, protein serine phosphatase activity has also been detected in extracts of Halobacterium salinarum (36) and Haloferax volcanii (320), but the enzymes responsible have not been identified.…”

Section: Archaeal Protein Kinases and Phosphatasesmentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

194

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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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“…reagents (45), while neither PP1-arch nor its presumed homologs from halophilic or methanogenic archaeons show sensitivity to any of a wide array of such compounds (17,29,30). PP1-arch from S. solfataricus also is insensitive to the classic PP1/2A/2B inhibitors okadaic acid, calyculin A, and microcystin LR (17).…”

Section: Discussionmentioning

confidence: 99%

“…This enzyme, the representative of a broadly distributed archaeal family of divalent metal ion-stimulated protein-serine/threonine phosphatases (17,29,30), bears remarkable resemblance to the predominant group of protein-serine/threonine phosphatases in the Eucarya, the PP1/2A/2B superfamily (3,7). This observation suggests that the archaeal and eucaryal members of this enzyme superfamily not only arose from a common ancestor but probably functioned as dedicated protein phosphatases prior to the divergence of these phylogenetic domains one from another.…”

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confidence: 99%

Isolation and cloning of a protein-serine/threonine phosphatase from an archaeon

et al. 1995

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A divalent metal ion-stimulated protein-serine/threonine phosphatase, PP1-arch, was purified approximately 1,000-fold from the extreme acidothermophilic archaeon Sulfolobus solfataricus (ATCC 35091). Purified preparations contained 40 to 70% of total protein as PP1-arch, as determined by assay-ing sodium dodecyl sulfatepolyacrylamide gels for protein phosphatase activity. The first 25 amino acids of the protein's sequence were identified, as well as an internal sequence spanning some 20 amino acids. Using this information, we cloned the gene for PP1-arch via the application of PCR and conventional cloning techniques. The gene for PP1-arch predicted a protein of 293 amino acids that bore striking resemblance to the members of the major family of protein-serine/threonine phosphatases from members of the domain Eucarya, the PP1/2A/2B superfamily. The core of the protein, spanning residues 4 to 275, possessed 29 to 31% identity with these eucaryal protein phosphatases. Of the 42 residues found to be absolutely conserved among the known eucaryal members of the PP1/2A/2B superfamily, 33 were present in PP1-arch. If highly conservative substitutions are included, this total reached 37. The great degree of sequence conservation between molecules from two distinct phylogenetic domains implies that the members of this enzyme superfamily had evolved as specialized, dedicated protein phosphatases prior to the divergence of members of the Archaea and Eucarya from one another.Protein phosphorylation-dephosphorylation represents a ubiquitous and prominent mechanism for regulating cellular processes. Protein kinases, protein phosphatases, and the phosphoproteins that they modify have been found in virtually every living organism. A priori, such universality might suggest that protein phosphorylation-dephosphorylation constitutes a very ancient means for exerting regulatory control. However, for many years, comparisons between the components of bacterial and eucaryal protein phosphorylation networks showed them to be structurally distinct, suggesting that each arose independently, at different times and places (reviewed in reference 18). For example, while all eucaryal protein kinases could be grouped into a single giant superfamily (14), the protein kinases from bacterial organisms showed no significant resemblance to this group (9). While members of the domain Eucarya phosphorylated some proteins on tyrosine residues, members of the domain Bacteria apparently did not (13). Therefore, it was and still is widely believed that protein phosphorylationdephosphorylation constitutes a relatively recent addition to the cell's regulatory repertoire, one that arose separately in each phylogenetic domain after it had diverged from its predecessors.Recent evidence has eroded the foundation upon which this consensus is based. Tyrosine-phosphorylated proteins have been detected in several members of the Bacteria (1,10,33,34,43). Genes encoding bacterial protein-histidine kinases have been discovered in eucaryal species ranging from rats (31...

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A Protein-Serine Phosphatase from the Halophilic Archaeon Haloferax volcanii

Cited by 21 publications

References 0 publications

Inhibition of an archaeal protein phosphatase activity by okadaic acid, microcystin‐LR, or calyculin A

Inhibition of an archaeal protein phosphatase activity by okadaic acid, microcystin‐LR, or calyculin A

Posttranslational Protein Modification inArchaea

Isolation and cloning of a protein-serine/threonine phosphatase from an archaeon

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