Regulation of archaella expression by the FHA and von Willebrand domain‐containing proteins ArnA and ArnB in <i>Sulfolobus acidocaldarius</i>

Reimann, Julia; Lassak, Kerstin; Khadouma, Sunia; Ettema, Thijs J. G.; Yang, Nuan; Driessen, Arnold J. M.; Klingl, Andreas; Albers, Sonja‐Verena

doi:10.1111/j.1365-2958.2012.08186.x

Cited by 64 publications

(132 citation statements)

References 32 publications

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“…However, the physiological function of this cascade was not elucidated until Reimann et al. (2012) showed that in S. acidocaldarius a regulatory system consisting of the homolog of ST0829, ArnA and various other proteins regulates expression of the motility structure, the archaellum. In S. acidocaldarius , an operon consisting of seven genes, which are expressed from two promoters encodes for the archaellum (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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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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“…However, distinct PilB and PilC paralogues are required for archaeal type IV pilus and flagella biosynthesis (Albers and Pohlschroder, 2009;Ghosh and Albers, 2011;Lassak et al, 2012). Consistent with having unique biosynthesis machineries, it has recently been shown that the transcriptional regulation of archaeal flagella and pili expression within biofilms is, as in bacteria, inversely related (Reimann et al, 2012;Lassak et al, 2013;Orell et al, 2013b).…”

Section: Introductionmentioning

confidence: 97%

A conserved type IV pilin signal peptide H‐domain is critical for the post‐translational regulation of flagella‐dependent motility

Esquivel

Pohlschröder

2014

Molecular Microbiology

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SummaryIn many bacteria and archaea, type IV pili facilitate surface adhesion, the initial step in biofilm formation. Haloferax volcanii has a specific set of adhesion pilins (PilA1-A6) that, although diverse, contain an absolutely conserved signal peptide hydrophobic (H) domain. Data presented here demonstrate that these pilins (PilA1-A6) also play an important role in regulating flagella-dependent motility, which allows cells to rapidly transition between planktonic and sessile states. Cells lacking adhesion pilins exhibit a severe motility defect, however, expression of any one of the adhesion pilins in trans can rescue the motility and adhesion. Conversely, while deleting pilB3-C3, genes required for PilA pilus biosynthesis, results in cells lacking pili and having an adhesion defect, it does not affect motility, indicating that motility regulation requires the presence of pilins, but not assembled pili. Mutagenesis studies revealed that the pilin-dependent motility regulatory mechanism does not require the diverse C-terminal region of the PilA pilins but specifically involves the conserved H-domain. This novel post-translational regulatory mechanism, which employs components that promote biofilm formation to inhibit motility, can provide a rapid response to changing environmental conditions. A model for this regulatory mechanism, which may also be present in other prokaryotes, is discussed.

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“…Furthermore, the first signal transduction pathway involved in archaella expression mediated by reversible protein phosphorylation was discovered in Sul. acidocaldarius (429,435) and Sul. tokodaii (436).…”

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

271

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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Regulation of archaella expression by the FHA and von Willebrand domain‐containing proteins ArnA and ArnB in Sulfolobus acidocaldarius

Cited by 64 publications

References 32 publications

Protein phosphorylation and its role in archaeal signal transduction

Protein phosphorylation and its role in archaeal signal transduction

A conserved type IV pilin signal peptide H‐domain is critical for the post‐translational regulation of flagella‐dependent motility

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

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