Haloarcula marismortui archaellin genes as ecoparalogs

Syutkin, Alexey S.; Pyatibratov, M. G.; Galzitskaya, Oxana V.; Rodrı́guez-Valera, Francisco; Fedorov, O.

doi:10.1007/s00792-013-0619-4

Cited by 22 publications

(21 citation statements)

References 32 publications

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“…The higher stability at high ionic strengths of archaella built exclusively of FlaB raises the question why in the wild‐type strain pNG100 encoded FlaA2 has substituted FlaB as major archaellin and what is the evolutionary advantage of maintaining FlaA2. It was shown previously that the archaellin FlaA2 is more stable at low ionic strengths (Syutkin, Pyatibratov, Galzitskaya, et al., ) and indeed the above described analysis shows that its expression is induced in media with 20% salinity. As especially low ionic strength causes stress to halophilic organisms, the presence of the FlaA2 archaellin, and specifically the possibility to adapt the occurrence of FlaB and FlaA2 in archaella, represents a distinct advantage.…”

Section: Discussionsupporting

confidence: 62%

“…Antibodies recognizing both the FlaA2 and FlaB protein were used for immunodetection (see M&M). FlaA2 and FlaB can be distinguished by their size on SDS polyacrylamide gels: FlaA, 47 kDa and FlaB, 48 kDa, (the archaellins of H. marismortui run differently on SDS‐gel because of their low pI and protein modifications, Pyatibratov et al., ; Syutkin, Pyatibratov, Galzitskaya, et al., ). In wild‐type cultures, we detected minor amounts of FlaB and higher levels of FlaA2, which is in correspondence with the qRT‐PCR results (Figures a and ).…”

Section: Resultsmentioning

confidence: 99%

“…The existence of this hook complex has been reported in one case, but no detailed studies on its composition or structure have been performed (Bardy, Mori, Komoriya, Aizawa, & Jarrell, ). Interestingly, a completely different explanation for the need of several archaellins came when studying the halophilic euryarchaeon Haloarcula marismortui (Syutkin, Pyatibratov, & Fedorov, ; Syutkin, Pyatibratov, Galzitskaya, Rodríguez‐Valera, & Fedorov, ).…”

Section: Introductionmentioning

confidence: 99%

“…In contrast, the archaella of the ΔpNG100 strain are built exclusively from the FlaB archaellin ( Figure 1). It was demonstrated that both archaellins are able to form functional archaella alone (Syutkin, Pyatibratov, Beznosov, & Fedorov, 2012;Syutkin, Pyatibratov, Galzitskaya, et al, 2014). However, the FlaB protein proved very stable at high ionic strengths, while the FlaA2 protein can better resist media with low ionic strengths.…”

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confidence: 99%

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Salt‐dependent regulation of archaellins in Haloarcula marismortui

et al. 2018

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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.

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Section: Discussionsupporting

confidence: 62%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Salt‐dependent regulation of archaellins in Haloarcula marismortui

et al. 2018

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“…Such a cytosolic ring is not found in the T4P machinery. Boxed inserts; tomographic surface representations of (A) the bacterium T. thermophilus (Gold et al, 2015) and (B) the archaeon P. furiosus (Daum et al, 2017 (Syutkin et al, 2014), suggesting that distinct filaments may exist. Questions remain as to whether the minor pilins/archaellins are found at specific or sporadic locations along the filament.…”

Section: The Filaments and Their Protomersmentioning

confidence: 99%

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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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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Haloarcula marismortui archaellin genes as ecoparalogs

Cited by 22 publications

References 32 publications

Salt‐dependent regulation of archaellins in Haloarcula marismortui

Salt‐dependent regulation of archaellins in Haloarcula marismortui

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

Archaellum

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