The activity of an ancient atypical protein kinase is stimulated by ADP-ribose in vitro

Haile, January D.; Kennelly, Peter J.

doi:10.1016/j.abb.2011.04.006

Cited by 11 publications

(20 citation statements)

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“…Intriguingly, ADP-ribose, the breakdown product of the poly(ADP-ribose) chains that covalently modify many eukaryal proteins, particularly those found in chromatin, markedly stabilized SsoPK5, an effect that could be enhanced by millimolar levels of 5Ј-AMP. Enhancement was highly specific to 5Ј-AMP and independent of autophosphorylation (51).…”

Section: The Sulfolobales Kinomementioning

confidence: 87%

“…tein exhibited detectable but relatively sluggish protein-serine/ threonine kinase activity toward acidic proteins such as casein and reduced carboxyamidomethylated and maleylated lysozyme (51). No activity was detected toward two basic proteins: histones and myelin basic protein.…”

Section: The Sulfolobales Kinomementioning

confidence: 98%

“…SsoPK5 also phosphorylated itself on serine and threonine. Substitution of Thr 159 , a predicted site of autophosphorylation, by alanine resulted in a 50% decrease in self-phosphorylation and loss of activity toward exogenous protein substrates (51). Intriguingly, ADP-ribose, the breakdown product of the poly(ADP-ribose) chains that covalently modify many eukaryal proteins, particularly those found in chromatin, markedly stabilized SsoPK5, an effect that could be enhanced by millimolar levels of 5Ј-AMP.…”

Section: The Sulfolobales Kinomementioning

confidence: 98%

“…An eIF2␣ protein kinase homolog from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 (Ph0512p) phosphorylates the archaeal homolog of eIF2␣ (aIF2␣) in vitro (53). Phosphorylation occurred on Ser 48 , which aligns with the site of regulatory protein phosphorylation in eIF2␣ (Ser 51 ). This serine residue is conserved in deduced aIF2␣ proteins in the archaea Methanococcus jannaschii, M. thermoautotrophicum, and Archaeoglobus fulgidus (53), as well as S. solfataricus (38).…”

Section: The Sulfolobales Kinomementioning

confidence: 99%

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Protein Ser/Thr/Tyr Phosphorylation in the Archaea

Kennelly

2014

Journal of Biological Chemistry

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The third domain of life, the Archaea (formerly Archaebacteria), is populated by a physiologically diverse set of microorganisms, many of which reside at the ecological extremes of our global environment. Although ostensibly prokaryotic in morphology, the Archaea share much closer evolutionary ties with the Eukarya than with the superficially more similar Bacteria. Initial genomic, proteomic, and biochemical analyses have revealed the presence of "eukaryotic" protein kinases and phosphatases and an intriguing set of serine-, threonine-, and tyrosine-phosphorylated proteins in the Archaea that may offer new insights into this important regulatory mechanism. A Maturing Evolutionary Perspective on Protein (De)phosphorylationFor several decades, the phosphorylation of proteins on serine and threonine residues was generally regarded as exclusively eukaryotic in origin and distribution, an adaptation to the coordination and communication requirements of a more complex compartmentalized cell form (1). In this scenario, tyrosine phosphorylation emerged to meet the expanded signal transduction needs of "higher" eukaryotes composed of multiple differentiated cells. The persistence and pervasiveness of this viewpoint are manifested by the continued use of the designator "eukaryotic protein kinase" (ePK) 2 when referring to homologs of the prototype for this superfamily, the catalytic subunit of the cAMP-dependent protein kinase.As the 1990s dawned, occasional reports surfaced indicating the presence of eukaryotic protein kinases and protein phosphatases in bacteria and viruses (1, 2). However, their close association with pathogenic organisms, tendency to target proteins endogenous to their eukaryotic hosts, and frequent coding by mobile elements such as plasmids were consistent with acquisition from the Eukarya by lateral gene transfer. It was not until genomics fueled a quantum leap in our understanding of the macromolecular populations within living organisms that it became apparent that many ostensibly eukaryotic protein kinases and protein phosphatases were in fact indigenous to some prokaryotes as well (3, 4). Early Studies on Protein Phosphorylation in the ArchaeaIn the late 1970s, the Archaea emerged as a new player in the exploitation of phylogenetic diversity for tracing the evolution of biological macromolecules (5). Although morphologically prokaryotic, the rRNA sequences of the Archaea were more closely related to those of the Eukarya than to the superficially similar Bacteria, indicating that the first divergence from the last universal common ancestor separated the bacterial line of descent from a conjoint eukaryal/archaeal one.The first indication that archaeal proteins were subject to regulation via covalent phosphorylation was reported by Spudich and Stoeckenius (6), who detected multiple radiolabeled polypeptides in extracts from cultures of the extreme halophile Halobacterium halobium that were grown in media containing 32 P-labeled inorganic phosphate. The radiolabel remained associated with the poly...

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Section: The Sulfolobales Kinomementioning

confidence: 87%

Section: The Sulfolobales Kinomementioning

confidence: 98%

Section: The Sulfolobales Kinomementioning

confidence: 98%

Section: The Sulfolobales Kinomementioning

confidence: 99%

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Protein Ser/Thr/Tyr Phosphorylation in the Archaea

Kennelly

2014

Journal of Biological Chemistry

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“…tokodaii, are the best-studied Archaea regarding protein phosphorylation. Four protein phosphatases (427)(428)(429) and five protein kinases (430)(431)(432)(433)(434) were identified and biochemically investigated. Furthermore, the first signal transduction pathway involved in archaella expression mediated by reversible protein phosphorylation was discovered in Sul.…”

Section: Regulation At the Protein Levelmentioning

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

280

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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Expanding the archaellum regulatory network - the eukaryotic protein kinases ArnC and ArnD influence motility ofSulfolobus acidocaldarius

et al. 2016

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Expression of the archaellum, the archaeal‐type IV pilus‐like rotating motility structure is upregulated under nutrient limitation. This is controlled by a network of regulators, called the archaellum regulatory network (arn). Several of the components of this network in Sulfolobus acidocaldarius can be phosphorylated, and the deletion of the phosphatase PP2A results in strongly increased motility during starvation, indicating a role for phosphorylation in the regulation of motility. Analysis of the motility of different protein kinase deletion strains revealed that deletion of saci_0965, saci_1181, and saci_1193 resulted in reduced motility, whereas the deletion of saci_1694 resulted in hypermotility. Here ArnC (Saci_1193) and ArnD (Saci_1694) are characterized. Purified ArnC and ArnD phosphorylate serine and threonine residues in the C‐terminus of the repressor ArnB. arnC is upregulated in starvation medium, whereas arnD is constitutively expressed. However, while differences in the expression and levels of flaB were observed in the ΔarnD strain during growth under rich conditions, under nutrient limiting conditions the ΔarnC and ΔarnD strains showed no large differences in the expression levels of the archaellum or of the studied regulators. This suggests that next to the regulation via the archaellum regulatory network additional regulatory mechanisms of expression and/or activity of the archaellum exist.

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The activity of an ancient atypical protein kinase is stimulated by ADP-ribose in vitro

Cited by 11 publications

References 50 publications

Protein Ser/Thr/Tyr Phosphorylation in the Archaea

Protein Ser/Thr/Tyr Phosphorylation in the Archaea

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

Expanding the archaellum regulatory network - the eukaryotic protein kinases ArnC and ArnD influence motility ofSulfolobus acidocaldarius

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