The archaeal flagellum: a different kind of prokaryotic motility structure

Thomas, Nikhil A.

doi:10.1016/s0168-6445(00)00061-9

Cited by 48 publications

(76 citation statements)

References 109 publications

(213 reference statements)

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“…In Archaea, cell motility mediated by flagella has been reported for representatives of the major phenotypic groups, i.e., the halophiles, the methanogens, the thermophiles, and the hyperthermophiles, largely based on microscopic investigation (20,184,436). Although fulfilling similar roles, archaeal flagella bear little resemblance to their bettercharacterized bacterial counterparts (7,265) in terms of structure or assembly.…”

Section: Fig 1 Schematic Depiction Of the Glycosylation Of Thementioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

196

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One of the first hurdles to be negotiated in the postgenomic era involves the description of the entire protein content of the cell, the proteome. Such efforts are presently complicated by the various posttranslational modifications that proteins can experience, including glycosylation, lipid attachment, phosphorylation, methylation, disulfide bond formation, and proteolytic cleavage. Whereas these and other posttranslational protein modifications have been well characterized in Eucarya and Bacteria, posttranslational modification in Archaea has received far less attention. Although archaeal proteins can undergo posttranslational modifications reminiscent of what their eucaryal and bacterial counterparts experience, examination of archaeal posttranslational modification often reveals aspects not previously observed in the other two domains of life. In some cases, posttranslational modification allows a protein to survive the extreme conditions often encountered by Archaea. The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by posttranslational modification in Archaea form the focus of this review

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Section: Fig 1 Schematic Depiction Of the Glycosylation Of Thementioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

196

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“…4). Moreover, mutational studies with M. voltae preFlaB (Thomas et al 2001a) and the S. solfataricus preGlcS (Albers and Driessen, unpublished observations) demonstrate that the archaeal peptidase is equipped with a specificity that is as broad as that observed for the bacterial enzyme. For the methanococcal preFlaB, it has been demonstrated that the positive charge at position -2 is absolutely required for cleavage (Thomas et al 2001b It therefore seems most likely that a single peptidase is responsible for processing of both the flagellins and the binding proteins.…”

Section: Type IV Pilin Peptidasesmentioning

confidence: 97%

“…The site of activity of PilD is the cytoplasmic site of the membrane. The presence of type IV pilin-like signal peptides implies the existence of a PilD homologue in archaea, but a candidate gene cannot be identified in S. solfataricus or other archaea by means of sequence similarity searching (Thomas et al 2001a). In vitro assays for the processing of flagellins (preFlaB) of M. voltae (Correia et al 2000) and binding proteins and flagellins in S. solfataricus (Albers and Driessen, unpublished observations) demonstrate that such an enzyme must be present.…”

Section: Type IV Pilin Peptidasesmentioning

confidence: 99%

“…In vitro assays for the processing of flagellins (preFlaB) of M. voltae (Correia et al 2000) and binding proteins and flagellins in S. solfataricus (Albers and Driessen, unpublished observations) demonstrate that such an enzyme must be present. It has been suggested that the archaeal type IV signal peptidase that is responsible for the processing of the preflagellins is distinct from the enzyme that processes the binding proteins (Thomas et al 2001a). This suggestion was based mainly on the observation that many of the known archaeal preflagellins are cleaved at a GA motif, whereas with binding proteins a GL or AI motif is prevalent.…”

Section: Type IV Pilin Peptidasesmentioning

confidence: 99%

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Signal peptides of secreted proteins of the archaeon Sulfolobus solfataricus : a genomic survey

Albers

Driessen

2002

Archives of Microbiology

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Signal peptides of secreted proteins of the archaeon Sulfolobus solfataricus: a genomic survey Albers, S.V.; Driessen, A.J.M. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 23-03-2019Abstract Analysis of the recently completed genome sequence of the thermoacidophilic archaeon Sulfolobus solfataricus reveals that about 4.2% of its proteome consists of putative secretory proteins with signal peptides. This includes members of the four major classes of signal peptides: secretory signal peptides, twin-arginine signal peptides, possible lipoprotein precursors, and type IV pilin signal peptides. The latter group is surprisingly large compared to the size of the groups in other organisms and seems to be used predominately for a subset of extracellular substrate-binding proteins.

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“…PG, peptidoglycan layer; SL, S-layer. (Adapted from Thomas et al, 2001; reprinted with permission from the Annual Review of Microbiology, volume 57 G 2003 by Annual Reviews www.annualreviews.org/).…”

Section: Glycoengineeringmentioning

confidence: 99%

Flagellar glycosylation – a new component of the motility repertoire?

2006

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The biosynthesis, assembly and regulation of the flagellar apparatus has been the subject of extensive studies over many decades, with considerable attention devoted to the peritrichous flagella of Escherichia coli and Salmonella enterica. The characterization of flagellar systems from many other bacterial species has revealed subtle yet distinct differences in composition, regulation and mode of assembly of this important subcellular structure. Glycosylation of the major structural protein, the flagellin, has been shown most recently to be an important component of numerous flagellar systems in both Archaea and Bacteria, playing either an integral role in assembly or for a number of bacterial pathogens a role in virulence. This review focuses on the structural diversity in flagellar glycosylation systems and demonstrates that as a consequence of the unique assembly processes, the type of glycosidic linkage found on archaeal and bacterial flagellins is distinctive. IntroductionThe bacterial flagellum, a key component of bacterial motility, is recognized as playing a vital role in the exquisite ability of many bacteria to adapt to the great diversity of biological niches in which they are found. This diversity includes aquatic and soil environments as well as the unique microenvironments which bacterial pathogens colonize within their respective protozoal, plant or animal host(s). While the model organisms for understanding the process of flagellar biosynthesis, assembly and regulation have been Salmonella enterica serovar Typhimurium strain LT2 and Escherichia coli K-12 (Aldridge & Hughes, 2002;Macnab, 2003), both of which produce peritrichous flagella composed of a single flagellin structural protein (simple flagella), recent post-genomic analysis has indicated that this existing paradigm reflects in general terms a degree of structural and regulatory conservation across the bacterial phyla (Pallen et al., 2005). However, the definitive contribution of the flagellar organelle to numerous unique bacterial lifestyles remains to be established. It is possible that the wellestablished paradigm defined by the motility systems of these two organisms may not be adequately encompassing for flagellar/motility systems from many distantly related bacterial species or indeed for alternative structures (lateral, polar or periplasmic flagella) of more closely related organisms. A recent body of work has described the process of flagellar glycosylation in a diverse number of bacterial species and in some cases has demonstrated a role for this process in both flagellar assembly and biological function. While it may be premature to consider glycosylation as a component of the flagellar repertoire, the intent of this review is to provide a current update on the extent of flagellar glycosylation in both Bacteria and Archaea, and to demonstrate that for a number of motile organisms it does appear to play a significant role both in flagellar assembly and in interactions of organisms with their surroundings. Flagellar structuresA va...

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The archaeal flagellum: a different kind of prokaryotic motility structure

Cited by 48 publications

References 109 publications

Posttranslational Protein Modification inArchaea

Posttranslational Protein Modification inArchaea

Signal peptides of secreted proteins of the archaeon Sulfolobus solfataricus : a genomic survey

Flagellar glycosylation – a new component of the motility repertoire?

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