Identification of a serine/threonine-specific protein phosphatase from the archaebacterium Sulfolobus solfataricus.

Kennelly, Peter J.; Oxenrider, Keith A.; Leng, Jie; Cantwell, John S.; Zhao, Ningyue

doi:10.1016/s0021-9258(18)53279-8

Cited by 36 publications

(9 citation statements)

References 38 publications

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“…The first evidence of protein phosphorylation in the Sulfolobales was reported in Sa. solfataricus (Kennelly et al 1993). PP activity was detected in soluble extracts of Sa.…”

Section: Protein Phosphorylation In Sa Solfataricusmentioning

confidence: 99%

The biology of thermoacidophilic archaea from the order Sulfolobales

Lewis

Recalde

Bräsen

et al. 2021

FEMS Microbiology Reviews

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Thermoacidophilic archaea belonging to the order Sulfolobales thrive in extreme biotopes, such as sulfuric hot springs and ore deposits. These microorganisms have been model systems for understanding life in extreme environments, as well as for probing the evolution of both molecular genetic processes and central metabolic pathways. Thermoacidophiles, such as the Sulfolobales, use typical microbial responses to persist in hot acid (e.g. motility, stress response, biofilm formation), albeit with some unusual twists. They also exhibit unique physiological features, including iron and sulfur chemolithoautotrophy, that differentiate them from much of the microbial world. Although first discovered more than 50 years ago, it was not until recently that genome sequence data and facile genetic tools have been developed for species in the Sulfolobales. These advances have not only opened up ways to further the probe novel features of these microbes, but have also paved the way for potential biotechnological applications. Discussed here are the nuances of the thermoacidophilic lifestyle of the Sulfolobales, including their evolutionary placement, cell biology, survival strategies, genetic tools, metabolic processes, and physiological attributes together with how these characteristics make thermoacidophiles ideal platforms for specialized industrial processes.

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“…The first evidence of protein phosphorylation in the Sulfolobales was reported in Sa. solfataricus (Kennelly et al 1993). PP activity was detected in soluble extracts of Sa.…”

Section: Protein Phosphorylation In Sa Solfataricusmentioning

confidence: 99%

The biology of thermoacidophilic archaea from the order Sulfolobales

Lewis

Recalde

Bräsen

et al. 2021

FEMS Microbiology Reviews

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“…The “EukaryoticPPP-Like” sequence set we identified by a HMM search in Archaea includes three members whose biochemistry has been characterized: PP1-arch ( Sulfolobus solfataricus ) 14 (UniProt:Q55059), PP1-arch2 ( Methanosarcina thermophila ) 15 , 16 (UniProt:O34200) and Py-PP1 ( Pyrodictium abyssi ) 17 (UniProt:O08367). Each of these has been demonstrated to have p-Ser/Thr activity.…”

Section: Discussionmentioning

confidence: 99%

The origin and radiation of the phosphoprotein phosphatase (PPP) enzymes of Eukaryotes

Kerk

Mattice

Valdés‐Tresanco

et al. 2021

Sci Rep

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Phosphoprotein phosphatase (PPP) enzymes are ubiquitous proteins involved in cellular signaling pathways and other functions. Here we have traced the origin of the PPP sequences of Eukaryotes and their radiation. Using a bacterial PPP Hidden Markov Model (HMM) we uncovered “BacterialPPP-Like” sequences in Archaea. A HMM derived from eukaryotic PPP enzymes revealed additional, unique sequences in Archaea and Bacteria that were more like the eukaryotic PPP enzymes then the bacterial PPPs. These sequences formed the basis of phylogenetic tree inference and sequence structural analysis allowing the history of these sequence types to be elucidated. Our phylogenetic tree data strongly suggest that eukaryotic PPPs ultimately arose from ancestors in the Asgard archaea. We have clarified the radiation of PPPs within Eukaryotes, substantially expanding the range of known organisms with PPP subtypes (Bsu1, PP7, PPEF/RdgC) previously thought to have a more restricted distribution. Surprisingly, sequences from the Methanosarcinaceae (Euryarchaeota) form a strongly supported sister group to eukaryotic PPPs in our phylogenetic analysis. This strongly suggests an intimate association between an Asgard ancestor and that of the Methanosarcinaceae. This is highly reminiscent of the syntrophic association recently demonstrated between the cultured Lokiarchaeal species Prometheoarchaeum and a methanogenic bacterial species.

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“…More recently, several examples of PPP family members encoded by the genomes of members of the Archaea and Bacteria have been characterized in some detail and their genes cloned and sequenced. They include PP1-arch1 from the thermophilic archaeon Sulfolobus solfataricus (83,84), PP1-arch2 from the methanogenic archaeon Methanosarcina thermophila TM-1 (85, 86), Py-PP1 from Pyrodictium abyssi TAG11 (87), PP1-cyano1 and PP1-cyano2 from the cyanobacteria Microcystis aeruginosa PCC7820 and M. aeruginosa UTEX2063, respectively (88,89), and PrpA and PrpB from E. coli (90). These prokaryotic representatives of the PPP family appear to share several properties in common.…”

Section: The Ppp Familymentioning

confidence: 99%

“…PP1-arch1 and PP1-arch2 exhibit high, approximately 30%, identity to the catalytic subunits of eukaryotic PP1 and PP2A and were active toward the phosphoseryl, but not the phosphotyrosyl, substrates against which they were tested (83)(84)(85)(86). By contrast, the four bacterial PPPs exhibited dual-specific protein phosphatase activity in vitro, hydrolyzing protein-bound phosphotyrosine, phosphoserine, and phosphothreonine (89,90).…”

Section: The Ppp Familymentioning

confidence: 99%

“…Few data are available concerning the physiological role of archaeal PPPs. Fractionation of extracts from laboratory cultures grown on rich media indicate that the archaeons S. solfataricus (83), M.thermophila TM-1 (85), and Haloferax volcanii (91) all contain a single dominant source of proteinserine/threonine phosphatase activity that has all the characteristics of a PPP family enzyme. The gene for Py-PP1 from P. abyssi is cotranscribed with a gene, canB, encoding a protein subunit of the unique, tubular extracellular network found in this archaeon -implying a role in the regulation or modification of network proteins (87).…”

Section: The Ppp Familymentioning

confidence: 99%

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Life among the primitives protein O-phosphatases in prokaryotes

Kennelly¹

1999

Front Biosci

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Prokaryotes contain at least five distinct families of protein O-phosphatases, including AceK, the chimeric isocitrate dehydrogenase kinase/phosphatase, and four protein phosphatase families first identified and characterized in Eukaryotes. The latter consist of the PPP and PPM families of protein-serine/threonine phosphatases, and the low molecular weight and conventional families of protein-tyrosine phosphatases. Prokaryotic protein Ophosphatases participate in the regulation of metabolic processes and the transduction of environmental signals.Certain pathogenic bacteria employ protein-tyrosine phosphatases as virulence factors, injecting them into host cells where they enzymatically perturb the phosphorylation state of proteins therein. While our understanding of protein O-phosphorylation events in Prokaryotes only now is emerging from its infancy, their phylogenetic diversity and malleability to genetic manipulation render these "simple'" organisms powerful vehicles for answering fundamental questions concerning the origins and evolution of this key biological regulatory mechanism.

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Identification of a serine/threonine-specific protein phosphatase from the archaebacterium Sulfolobus solfataricus.

Cited by 36 publications

References 38 publications

The biology of thermoacidophilic archaea from the order Sulfolobales

The biology of thermoacidophilic archaea from the order Sulfolobales

The origin and radiation of the phosphoprotein phosphatase (PPP) enzymes of Eukaryotes

Life among the primitives protein O-phosphatases in prokaryotes

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