High‐resolution archaellum structure reveals a conserved metal‐binding site

Meshcheryakov, V. A.; Shibata, Satoshi; Schreiber, Makoto; Villar‐Briones, Alejandro; Jarrell, Kenneth F; Aizawa, Shin‐Ichi; Wolf, Matthias

doi:10.15252/embr.201846340

Cited by 30 publications

(44 citation statements)

References 60 publications

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“…Recently, high resolution structures of archaellar filaments of methanogens and hyperthermophilic euryarchaea became available (Poweleit et al, 2016;Daum et al, 2017;Meshcheryakov et al, 2019). In these structures only a single type of archaellin is present in the filament, even though several archaellin genes are present in the genome.…”

Section: Discussionmentioning

confidence: 99%

“…Fundamental differences between archaeal and bacterial flagellar filaments are the presence of signal sequences in archaeal flagellins (archaellins) and the multiplicity of archaellin encoding genes in archaea (Jarrell and Albers, 2012). Recently, cryoelectron microscopy was used to determine the spatial structures of the archaella filaments of three archaea: two methanogenes Methanospirillum hungatei (3.4 Å resolution) (Poweleit et al, 2016) and Methanococcus maripaludis (4 Å resolution) (Meshcheryakov et al, 2019) and a hyperthermophile Pyrococcus furiosus (4.2 Å resolution) (Daum et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

“…Methanocaldococcus jannaschii has been determined at a resolution of 1.5 Å (Meshcheryakov et al, 2019). The structure of archaeal filaments differs significantly not only from bacterial flagella, but also from bacterial type IV pili (Braun et al, 2016;Poweleit et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

“…The proposed models of spatial archaellar filament structure do not explain the structural and functional role of multiple archaellins. Despite the presence of several archaellin genes in genomes of M. hungatei, M. maripaludis and P. furiosus, protein products of only one of these genes were found incorporated in their filaments (Poweleit et al, 2016;Daum et al, 2017;Meshcheryakov et al, 2019). This raises the question about the importance of encoding multiple different archaellins.…”

Section: Introductionmentioning

confidence: 99%

“…Inactivation of either the flaB1 or flaB2 genes resulted in loss of motility and cessation of archaellum synthesis (including the hook) (Chaban et al, 2007). Recently, it has been shown that FlaB1 is the predominant component of Methanococcus maripaludis filaments (Meshcheryakov et al, 2019). Inactivation of the flaB3 gene does not lead to the cessation of filament synthesis and a noticeable change in motility on semiliquid agar (Chaban et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Interaction of two strongly divergent archaellins stabilizes the structure of theHalorubrumarchaellum

Pyatibratov

Syutkin

Quax

et al. 2019

Preprint

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# Co-first authorsRunning Title: Two-component composition stabilizes Halorubrum archaella SUMMARYThe archaellum is a unique motility structure that has only functional similarity to its bacterial counterpart, the flagellum. Archaellar filaments consist of thousands of copies of the protein protomer archaellin. Most euryarchaeal genomes encode multiple homologous archaellins. The role of these multiple archaellin genes remains unclear. Halophilic archaea from the genus Halorubrum possess two archaellin genes, flaB1 and flaB2. Amino acid sequences of the corresponding protein products are extraordinarily diverged (identity of ~ 40%). To clarify roles for each archaellin, we compared archaella from two natural Halorubrum lacusprofundi strains: the DL18 strain, which possesses both archaellin genes, and the type strain ACAM 34 whose genome contains the flaB2 gene only. Both strains synthesize functional archaella; however, the DL18 strain, where both archaellins are present in comparable amounts, is more motile. In addition, we expressed these different Hrr. lacusprofundi archaellins in a Haloferax volcanii strain from which the endogenous archaellin genes were deleted. Three Hfx. volcanii strains expressing Hrr. lacusprofundi archaellins flaB1, flaB2 or flaB1-flaB2 produced archaellum filaments consisting of only one (FlaB1 or FlaB2) or both (FlaB1/B2) archaellins. All three recombinant Hfx. volcanii strains were motile, although there were profound differences in the efficiency of motility. The recombinant filaments resemble the natural filaments of Hrr. lacusprofundi. Electron microscopy showed that FlaB1 FlaB2-archaella look like typical supercoiled filaments, while with the shape of the FlaB1-and FlaB2-archaella is more variable. Both native and recombinant FlaB1 FlaB2-filaments have greater thermal stability and are more resistant to low salinity stress than single-component filaments. This shows that thermal stability of archaellins depends on the presence of both archaellin types, indicating a close interaction between these subunits in the supramolecular structure. Functional helical Hrr. lacusprofundi archaella can be composed of either single archaellin: FlaB2 or FlaB1; however, the two divergent archaellin subunits in combination provide additional stabilization to the archaellum structure and thus adaptation to a wider range of external conditions. A comparative genomic analysis of archaellins suggests that the described combination of divergent archaellins is not restricted to Hrr. lacusprofundi, but is occurring also in organisms from other haloarchaeal genera.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Interaction of two strongly divergent archaellins stabilizes the structure of theHalorubrumarchaellum

Pyatibratov

Syutkin

Quax

et al. 2019

Preprint

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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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Interaction of two strongly divergent archaellins stabilizes the structure of the Halorubrum archaellum

et al. 2020

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Halophilic archaea from the genus Halorubrum possess two extraordinarily diverged archaellin genes, flaB1 and flaB2 . To clarify roles for each archaellin, we compared two natural Halorubrum lacusprofundi strains: One of them contains both archaellin genes, and the other has the flaB2 gene only. Both strains synthesize functional archaella; however, the strain, where both archaellins are present, is more motile. In addition, we expressed these archaellins in a Haloferax volcanii strain from which the endogenous archaellin genes were deleted. Three Hfx. volcanii strains expressing Hrr. lacusprofundi archaellins produced functional filaments consisting of only one (FlaB1 or FlaB2) or both (FlaB1/FlaB2) archaellins. All three strains were motile, although there were profound differences in the efficiency of motility. Both native and recombinant FlaB1/FlaB2 filaments have greater thermal stability and resistance to low salinity stress than single‐component filaments. Functional supercoiled Hrr. lacusprofundi archaella can be composed of either single archaellin: FlaB2 or FlaB1; however, the two divergent archaellin subunits provide additional stabilization to the archaellum structure and thus adaptation to a wider range of external conditions. Comparative genomic analysis suggests that the described combination of divergent archaellins is not restricted to Hrr. lacusprofundi, but is occurring also in organisms from other haloarchaeal genera.

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High‐resolution archaellum structure reveals a conserved metal‐binding site

Cited by 30 publications

References 60 publications

Interaction of two strongly divergent archaellins stabilizes the structure of theHalorubrumarchaellum

Interaction of two strongly divergent archaellins stabilizes the structure of theHalorubrumarchaellum

Archaellum

Interaction of two strongly divergent archaellins stabilizes the structure of the Halorubrum archaellum

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