Structure and in situ organisation of the Pyrococcus furiosus archaellum machinery

Daum, Bertram; Vonck, Janet; Bellack, Annett; Chaudhury, Paushali; Reichelt, Robert; Albers, Sonja‐Verena; Rachel, Reinhard; Kühlbrandt, Werner

doi:10.7554/elife.27470

Cited by 76 publications

(173 citation statements)

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“…Studies have revealed a high degree of conservation, with similar post-translational modifications also observed in other Neisseria strains (Stimson et al, 1995;Craig et al, 2006). Archaella from Pyrococcus furiosus, possess five N-linked glycosylation sites in each FlaB 0 archaellin (Daum et al, 2017), while the Methanospirillum hungatei filament possesses six O-linked and two N-linked glycans per subunit (Poweleit et al, 2016).…”

Section: The Filaments and Their Protomersmentioning

confidence: 54%

“…These extend from the cell up to several micrometres in length and are predominantly found in polar regions (Bardy et al, 2002;Nudleman et al, 2006;Gold et al, 2015;Daum et al, 2017) (Figure 1), presumably ensuring co-ordinated and directional movement. Pilins and archaellins are synthesised typically as membrane-integral preproteins that contain a conserved class III signal sequence.…”

Section: The Filaments and Their Protomersmentioning

confidence: 99%

“…Pilins and archaellins share a characteristic 'lollipop' shape consisting of a hydrophobic N-terminal kinked α-helix followed by a C-terminal β-strand rich globular domain (Figure 2) (Braun et al, 2016;Kolappan et al, 2016;Poweleit et al, 2016;Daum et al, 2017;Wang et al, 2017). Differences in the sizes of individual monomers lead to variations in the filament packing and diameters of the assembled filaments (Braun et al, 2016;Kolappan et al, 2016;Poweleit et al, 2016;Daum et al, 2017;Wang et al, 2017).…”

Section: The Filaments and Their Protomersmentioning

confidence: 99%

“…Differences in the sizes of individual monomers lead to variations in the filament packing and diameters of the assembled filaments (Braun et al, 2016;Kolappan et al, 2016;Poweleit et al, 2016;Daum et al, 2017;Wang et al, 2017). The central core of the filament is formed from bundles of the N-terminal α-helices of individual monomers (Figure 2).…”

Section: The Filaments and Their Protomersmentioning

confidence: 99%

“…Bacteria and archaea can possess multiple pilin/archaellinlike proteins within their genome, often encoded in the same operon. However, the filaments seem to be comprised of one major form: PilA/PilE in bacteria (Gold and Brought to you by | University of Exeter Authenticated Download Date | 7/4/18 12:21 PM Kudryashev, 2016), and members of the FlaB family in archaea, such as FlaB 0 in P. furiosus (Daum et al, 2017) and FlaB 3 in M. hungatei (Poweleit et al, 2016). T4P can also be classified into T4aP and T4bP subgroups, based on their major pilin protein (in particular the length of leader peptide) and the organisation of their pilus genes (Pelicic, Schematic views of (A) the T4P and (B) the archaellum machinery highlights similarities (outlined in black and red) and differences (not outlined) in protein composition.…”

Section: The Filaments and Their Protomersmentioning

confidence: 99%

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

Daum

Gold

2018

Biological Chemistry

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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.

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Section: The Filaments and Their Protomersmentioning

confidence: 54%

Section: The Filaments and Their Protomersmentioning

confidence: 99%

Section: The Filaments and Their Protomersmentioning

confidence: 99%

Section: The Filaments and Their Protomersmentioning

confidence: 99%

Section: The Filaments and Their Protomersmentioning

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

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Archaellum

Jarrell¹,

Tripp²,

Albers³

2020

Encyclopedia of Life Sciences

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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.

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Archaeal Cells

Chadha¹,

Seydel²,

Klingl³

2020

Encyclopedia of Life Sciences

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At a first glance, Archaea are quite similar to Bacteria on a structural level, and for a long time they were named ‘Archaebacteria’. They can form cocci, rods, spirals or irregular shaped cells and are equally sized as Bacteria. Together they are referred to as ‘Prokaryotes’ because neither Archaea nor Bacteria possess a nucleus. Although this term indeed might be helpful in habitual language use, it does not refer to a phylogenetic group. In fact, transcription and translation machineries of Archaea have much more in common with eukaryotic cells than with Bacteria. In addition, there are many features that remain characteristic for Archaea, given by the fact that many representatives live and thrive under extreme environmental conditions. Key Concepts By application of respective PCR techniques, Archaea can be found in almost every habitat and sometimes are even more abundant than bacteria. Archaea show special adaptations to their sometimes extreme environments, like caldarchaeols, which are more stable at high temperatures. Like Bacteria, Archaea are also surrounded by a lipid bilayer, but in the latter case, the lipid moiety consists of C 5 ‐isoprenoid units that are coupled to glycerol via ether bonds at (sn)‐2,3 positions of the glycerol. Cell walls can be as simple as a proteinaceous surface layer or as complicated as in some methanogens with multiple layers, additional sheaths enclosing several cells and even more complex cell wall compounds. Archaea exhibit a broad variety in cell appendages that are different from bacterial ones in fine structure, composition, biosynthesis and anchorage in the cell.

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Structure and in situ organisation of the Pyrococcus furiosus archaellum machinery

Cited by 76 publications

References 73 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

Archaellum

Archaeal Cells

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