Archaeal Eukaryote-Like Serine/Threonine Protein Kinase Interacts with and Phosphorylates a Forkhead-Associated-Domain-Containing Protein

Wang, Bin; Yang, Sen; Zhang, Lei; He, Zheng‐Guo

doi:10.1128/jb.01471-09

Cited by 23 publications

(23 citation statements)

References 39 publications

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“…2010). All of them contained the catalytic loop (DVKPSN), the DFG motif and the conserved residues K 166 , D 287 and D 314 known from classical eukaryotic homologs (see Fig.…”

Section: Ser Thr and Tyr Phosphorylation In Archaeamentioning

confidence: 99%

Protein phosphorylation and its role in archaeal signal transduction

Esser

Hoffmann

Pham

et al. 2016

FEMS Microbiology Reviews

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Reversible protein phosphorylation is the main mechanism of signal transduction that enables cells to rapidly respond to environmental changes by controlling the functional properties of proteins in response to external stimuli. However, whereas signal transduction is well studied in Eukaryotes and Bacteria, the knowledge in Archaea is still rather scarce. Archaea are special with regard to protein phosphorylation, due to the fact that the two best studied phyla, the Euryarchaeota and Crenarchaeaota, seem to exhibit fundamental differences in regulatory systems. Euryarchaeota (e.g. halophiles, methanogens, thermophiles), like Bacteria and Eukaryotes, rely on bacterial-type two-component signal transduction systems (phosphorylation on His and Asp), as well as on the protein phosphorylation on Ser, Thr and Tyr by Hanks-type protein kinases. Instead, Crenarchaeota (e.g. acidophiles and (hyper)thermophiles) only depend on Hanks-type protein phosphorylation. In this review, the current knowledge of reversible protein phosphorylation in Archaea is presented. It combines results from identified phosphoproteins, biochemical characterization of protein kinases and protein phosphatases as well as target enzymes and first insights into archaeal signal transduction by biochemical, genetic and polyomic studies.

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“…2010). All of them contained the catalytic loop (DVKPSN), the DFG motif and the conserved residues K 166 , D 287 and D 314 known from classical eukaryotic homologs (see Fig.…”

Section: Ser Thr and Tyr Phosphorylation In Archaeamentioning

confidence: 99%

Protein phosphorylation and its role in archaeal signal transduction

Esser

Hoffmann

Pham

et al. 2016

FEMS Microbiology Reviews

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“…Moreover, at least one of the eight potential ePKs identified, the protein product of st1565, resembles the typical ePKs that predominate in eukaryotes (54). Using two-hybrid screens and pulldown assays, it was determined that the ST1565 protein kinase complexes with the protein product of st0829, a forkhead-associated (FHA) domain-containing transcription factor that interacts with the promoter region of a gene cluster encoding flagella-like proteins (55).…”

Section: The Sulfolobales Kinomementioning

confidence: 99%

“…The FHA domain-containing protein was initially implicated by its capacity to bind to and to physically interact with a typical ePK, the product of ORF st1565 from S. tokodaii (54). Subsequent analysis quickly revealed that the FHA domain-containing protein was phosphorylated by the ST1565 ePK in vitro, although the identity and location of the amino acid residue modified were not determined.…”

Section: The Sulfolobales Phosphoproteomementioning

confidence: 99%

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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“…St0829 of Sulfolobus tokodaii was demonstrated to be a Ser/Thr‐specific kinase that phosphorylates the forkhead‐associated (FHA) domain‐containing protein St1565. Unphosphorylated St1565 binds to the promoter region of the operon encoding the archaellum, while phosphorylation inhibits binding (Duan & He, ; Wang, Yang, Zhang, & He, ). However, the physiological function of this kinase remains unclear.…”

Section: Introductionmentioning

confidence: 99%

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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Archaeal Eukaryote-Like Serine/Threonine Protein Kinase Interacts with and Phosphorylates a Forkhead-Associated-Domain-Containing Protein

Cited by 23 publications

References 39 publications

Protein phosphorylation and its role in archaeal signal transduction

Protein phosphorylation and its role in archaeal signal transduction

Protein Ser/Thr/Tyr Phosphorylation in the Archaea

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

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