Activation of SsoPK4, an Archaeal eIF2α Kinase Homolog,  by Oxidized CoA

Ray, W. Keith; Potters, Mark; Haile, January D.; Kennelly, Peter J.

doi:10.3390/proteomes3020089

Cited by 8 publications

(17 citation statements)

References 67 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, ArnS could be required to phosphorylate an initiation factor required to translate starvation induced mRNAs. Indeed, SsoPK4 (Sso3182), ArnS closest homolog in S. solfataricus, can phosphorylate archaeal translation factor 2a (aIF2a) in vitro (Ray et al, 2015). In addition, S. acidocaldarius aIF2a (Saci_1275) was phosphorylated at Thr and Tyr residues in the phosphatase deletion strain, Dptp, but not in the hypermotile strain, Dpp2a, which suggests that it is differentially regulated (Reimann et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

ArnS, a kinase involved in starvation‐induced archaellum expression

Haurat

Figueiredo

Hoffmann

et al. 2016

Molecular Microbiology

View full text Add to dashboard Cite

Summary Organisms have evolved motility organelles that allow them to move to favourable habitats. Cells integrate environmental stimuli into intracellular signals to motility machineries to direct this migration. Many motility organelles are complex surface appendages that have evolved a tight, hierarchical regulation of expression. In the crenearchaeon Sulfolobus acidocaldarius, biosynthesis of the archaellum is regulated by regulatory network proteins that control expression of archaellum components in a phosphorylation‐dependent manner. A major trigger for archaellum expression is nutrient starvation, but although some components are known, the regulatory cascade triggered by starvation is poorly understood. In this work, the starvation‐induced Ser/Thr protein kinase ArnS (Saci_1181) which is located proximally to the archaellum operon was identified. Deletion of arnS results in reduced motility, though the archaellum is properly assembled. Therefore, our experimental and modelling results indicate that ArnS plays an essential role in the precisely controlled expression of archaellum components during starvation‐induced motility in Sulfolobus acidocaldarius. Furthermore they combined in vivo experiments and mathematical models to describe for the first time in archaea the dynamics of key regulators of archaellum expression.

show abstract

Section: Discussionmentioning

confidence: 99%

ArnS, a kinase involved in starvation‐induced archaellum expression

Haurat

Figueiredo

Hoffmann

et al. 2016

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

“…2010; Ray et al. 2015). Residues labeled in red and green have been identified in STK_15650 by combined mutational and in vitro studies and revealed to be essential for function or to decrease kinase activity, respectively (Wang et al.…”

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

View full text Add to dashboard Cite

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.

show abstract

“…Surprisingly little is known about phosphorylation in archaea even though most of the sequenced genomes encode typical and atypical ePKs as well as protein phosphatases (Esser & Siebers, ; Esser et al., ). The biochemical properties of ePKs of S. solfataricus , S. tokodaii, and S. acidocaldarius were characterized with respect to their kinase activities (Haile & Kennelly, ; Lower & Kennelly, , ; Lower et al., , ; Ray et al., ), but still little is known about which proteins are the natural targets of the kinase and how these proteins function in vivo . Here, we set out to identify possible protein kinases that play a role in the regulation of motility.…”

Section: Discusssionmentioning

confidence: 99%

“…properties of ePKs of S. solfataricus, S. tokodaii, and S. acidocaldarius were characterized with respect to their kinase activities (Haile & Kennelly, 2011;Lower & Kennelly, 2002, 2003Lower et al, 2000Lower et al, , 2004Ray et al, 2015), but still little is known about which proteins are the natural targets of the kinase and how these proteins function in vivo. Here, we set out to identify possible protein kinases that play a role in the regulation of motility.…”

Section: Discusssionmentioning

confidence: 99%

“…Our knowledge of crenarchaeal ePKs derives mainly from studies performed on kinases of S. solfataricus. Several ePKs and an aPK of S. solfataricus have been characterized with respect to their substrate specificity, ion preference as well as autophosphorylation and phosphotransfer activities to various exogenous substrates as, for example, casein (Haile & Kennelly, 2011;Lower, Bischoff, & Kennelly, 2000;Lower & Kennelly, 2002, 2003Lower, Potters, & Kennelly, 2004;Ray, Potters, Haile, & Kennelly, 2015). However, little is known about which proteins are the natural targets of these kinases.…”

mentioning

confidence: 99%

See 1 more Smart Citation

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

et al. 2016

View full text Add to dashboard Cite

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.

show abstract

Activation of SsoPK4, an Archaeal eIF2α Kinase Homolog, by Oxidized CoA

Cited by 8 publications

References 67 publications

ArnS, a kinase involved in starvation‐induced archaellum expression

ArnS, a kinase involved in starvation‐induced archaellum expression

Protein phosphorylation and its role in archaeal signal transduction

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

Contact Info

Product

Resources

About