Morphology of the archaellar motor and associated cytoplasmic cone in
            <i>Thermococcus kodakaraensis</i>

Briegel, Ariane; Oikonomou, Catherine M.; Chang, Yi‐Wei; Kjær, Andreas; Huang, Audrey; Kim, Ki-Woo; Ghosal, Debnath; Nguyen, Hong Hanh; Kenny, Dorothy; Loo, Rachel R. Ogorzalek; Gunsalus, Robert P.; Jensen, Grant J.

doi:10.15252/embr.201744070

Cited by 39 publications

(61 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the coccoid cyanobacterium Synechocystis however, the PilB ATPase was shown to concentrate in crescents adjacent to the plasma membrane, correlating strongly with the direction of twitching motility (Schuergers et al, 2015). In line with this, the archaeal cytosolic ring (putatively comprised of FlaC, FlaD and FlaE) is juxtaposed to the crescent-shaped polar cap organising centre (Briegel et al, 2017;Daum et al, 2017).…”

Section: To Twitch Versus Swimmentioning

confidence: 76%

“…Bacterial and archaeal membrane lipids are distinct, thus it is plausible that assembly of filaments in membranes could require different capabilities and thus evolution of different facilitator proteins. The difference in regulatory proteins is clearly owed to functional diversification, but the lack of the large periplasmic conduit in archaea studied so far (Briegel et al, 2017;Daum et al, 2017) may reflect a bacterial evolutionary pressure owing to the emergence of the outer membrane.…”

Section: To Twitch Versus Swimmentioning

confidence: 99%

“…PilQ-like conduits do not exist in archaea studied to date, including the species P. furiosus (Daum et al, 2017) and Thermococcus kodakarensis (Briegel et al, 2017), which are both surrounded by a single membrane and an S-layer ( Figures 1B and 3C). Instead of a conduit through the periplasm, the archaella traverse a gap in the S-layer (Daum et al, 2017), which may be the result of mechanical replacement or proteolytic degradation during filament assembly.…”

Section: Conduits and Accessory Proteinsmentioning

confidence: 99%

“…FlaC, FlaD and FlaE have been shown to interact with chemoreceptors via adaptor proteins (Schlesner et al, 2009), suggesting that they convey chemotropic signals to the motor complex. Interestingly, these cytosolic rings co-localise with a structure called the polar cap, which has been proposed to act as an organising centre for archaellar bundles (Briegel et al, 2017;Daum et al, 2017) (Figure 3C). In crenarchaeota such as Sulfolobus acidocaldarius, the FlaJ/I/H core is surrounded by a membrane-anchored oligomeric ring of FlaX proteins, which has been suggested to form the static part for archaellum force generation and recruitment of FlaB into the filament (Banerjee et al, 2012).…”

Section: Conduits and Accessory Proteinsmentioning

confidence: 99%

See 3 more Smart Citations

Twitch or swim: towards the understanding of prokaryotic motion based on the type IV pilus blueprint

Daum

Gold

2018

Biological Chemistry

View full text Add to dashboard Cite

Bacteria and archaea are evolutionarily distinct prokaryotes that diverged from a common ancestor billions of years ago. However, both bacteria and archaea assemble long, helical protein filaments on their surface through a machinery that is conserved at its core. In both domains of life, the filaments are required for a diverse array of important cellular processes including cell motility, adhesion, communication and biofilm formation. In this review, we highlight the recent structures of both the type IV pilus machinery and the archaellum determined in situ. We describe the current level of functional understanding and discuss how this relates to the pressures facing bacteria and archaea throughout evolution.

show abstract

Section: To Twitch Versus Swimmentioning

confidence: 76%

Section: To Twitch Versus Swimmentioning

confidence: 99%

Section: Conduits and Accessory Proteinsmentioning

confidence: 99%

Section: Conduits and Accessory Proteinsmentioning

confidence: 99%

See 2 more Smart Citations

Twitch or swim: towards the understanding of prokaryotic motion based on the type IV pilus blueprint

Daum

Gold

2018

Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…In contrast to the regulation of archaellation, the structure and biochemical composition of the archaellum have lately been mapped in increasingly greater detail (Banerjee, Neiner, Tripp, & Albers, ; Banerjee et al., ; Briegel et al., ; Chaudhury et al., ; Daum et al., ; Poweleit et al., ; Reindl et al., ). The protein components of the archaellum are quite conserved amongst motile archaea.…”

Section: Introductionmentioning

confidence: 99%

Salt‐dependent regulation of archaellins in Haloarcula marismortui

et al. 2018

View full text Add to dashboard Cite

Microorganisms require a motility structure to move towards optimal growth conditions. The motility structure from archaea, the archaellum, is fundamentally different from its bacterial counterpart, the flagellum, and is assembled in a similar fashion as type IV pili. The archaellum filament consists of thousands of copies of N‐terminally processed archaellin proteins. Several archaea, such as the euryarchaeon Haloarcula marismortui , encode multiple archaellins. Two archaellins of H. marismortui display differential stability under various ionic strengths. This suggests that these proteins behave as ecoparalogs and perform the same function under different environmental conditions. Here, we explored this intriguing system to study the differential regulation of these ecoparalogous archaellins by monitoring their transcription, translation, and assembly into filaments. The salt concentration of the growth medium induced differential expression of the two archaellins. In addition, this analysis indicated that archaellation in H. marismortui is majorly regulated on the level of secretion, by a still unknown mechanism. These findings indicate that in archaea, multiple encoded archaellins are not completely redundant, but in fact can display subtle functional differences, which enable cells to cope with varying environmental conditions.

show abstract

Archaellum

Jarrell¹,

Tripp²,

Albers³

2020

Encyclopedia of Life Sciences

View full text Add to dashboard Cite

Each of the three domains of life contains its own unique swimming apparatus. The archaellum (formerly called archaeal flagellum) is a unique, ‘tail‐like’ structure used for motility by single‐celled organisms belonging to the domain Archaea. Although archaella are functionally similar to the flagella found on bacteria, they differ significantly in structure and mode of assembly. Archaella are evolutionarily related to type IV pili, and each of the two systems shares several key homologues required for assembly of the respective structures. Recent studies have contributed much to our knowledge concerning the regulation of the operon encoding the archaellum proteins. In addition, the elucidation of the structures of most of the Fla proteins involved in archaella structure and function, coupled with detailed atomic models of the archaellum, including the motor, has provided major insights into how this unique motility organelle is assembled and functions, often in harsh environments inhabited by many archaea. Key Concepts Each of the three domains of life has a unique motility apparatus, which have recently been assigned distinct names (Archaea: archaellum; Bacteria: flagellum and Eukaryotes: cilium). The archaellum is functionally equivalent to flagellum but is evolutionarily related to a type IV pilus, with the archaella and type IV pili systems sharing important homologues. Archaea have the ability to regulate the synthesis of archaella depending on growth conditions, such as available nutrients and temperature. There can be crosstalk in the regulation of archaella with adhesive pili, allowing the cells under certain conditions to make only one type of appendage, either for swimming or adhesion. N‐Glycosylation of the major filament proteins, the archaellins, is widespread and essential under normal conditions for assembly of filaments. The ATPase responsible for assembly of the archaellins into the filament, that is, FlaI, is also responsible for the hydrolysis of ATP that powers the rotation of archaella. In many archaea, the archaellum interacts with a bacterial‐like chemotaxis system that requires novel chemotaxis proteins to act as adaptors to connect the systems. Not all archaellated species have an associated chemotaxis system. Knowledge of the structure and assembly of archaella has greatly increased in the past 5 years with atomic models of several archaella structures as well as structures of most of the individual archaella proteins and their interaction partners.

show abstract

Morphology of the archaellar motor and associated cytoplasmic cone in Thermococcus kodakaraensis

Cited by 39 publications

References 50 publications

Twitch or swim: towards the understanding of prokaryotic motion based on the type IV pilus blueprint

Twitch or swim: towards the understanding of prokaryotic motion based on the type IV pilus blueprint

Salt‐dependent regulation of archaellins in Haloarcula marismortui

Archaellum

Contact Info

Product

Resources

About