Results 1 to 10 of about 202 (79)

Interaction of two strongly divergent archaellins stabilizes the structure of the Halorubrum archaellum [PDF]

open access: yesMicrobiologyOpen, 2020
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 ...
Alexey Syutkin   +2 more
exaly   +10 more sources

Salt-dependent regulation of archaellins in Haloarcula marismortui [PDF]

open access: yesMicrobiologyOpen, 2019
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
Alexey Syutkin   +2 more
exaly   +10 more sources

Pilin Processing Follows a Different Temporal Route than That of Archaellins in Methanococcus maripaludis [PDF]

open access: yesLife, 2015
Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism.
Ken F Jarrell, Divya B Nair
exaly   +6 more sources

Effects of N-glycosylation site removal in archaellins on the assembly and function of archaella in Methanococcus maripaludis. [PDF]

open access: yesPLoS ONE, 2015
In Methanococcus maripaludis S2, the swimming organelle, the archaellum, is composed of three archaellins, FlaB1S2, FlaB2S2 and FlaB3S2. All three are modified with an N-linked tetrasaccharide at multiple sites.
Yan Ding   +7 more
doaj   +6 more sources

N-Glycosylation Is Important for Halobacterium salinarum Archaellin Expression, Archaellum Assembly and Cell Motility [PDF]

open access: yesFrontiers in Microbiology, 2019
Halobacterium salinarum are halophilic archaea that display directional swimming in response to various environmental signals, including light, chemicals and oxygen. In Hbt. salinarum, the building blocks (archaellins) of the archaeal swimming apparatus (
Marianna Zaretsky   +4 more
doaj   +4 more sources

Complementation of an aglB Mutant of Methanococcus maripaludis with Heterologous Oligosaccharyltransferases [PDF]

open access: yesPLoS ONE, 2016
The oligosaccharyltransferase is the signature enzyme for N-linked glycosylation in all domains of life. In Archaea, this enzyme termed AglB, is responsible for transferring lipid carrier-linked glycans to select asparagine residues in a variety of ...
Ken F Jarrell   +2 more
exaly   +3 more sources

Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway [PDF]

open access: yesFrontiers in Microbiology, 2021
Whereas N-glycosylation is a seemingly universal process in Archaea, pathways of N-glycosylation have only been experimentally verified in a mere handful of species.
Zlata Vershinin   +3 more
doaj   +2 more sources

SaUspA, the Universal Stress Protein of Sulfolobus acidocaldarius Stimulates the Activity of the PP2A Phosphatase and Is Involved in Growth at High Salinity

open access: yesFrontiers in Microbiology, 2020
In Sulfolobus acidocaldarius, the protein phosphatase PP2A plays important regulatory roles in many cellular processes, including cell growth, cell shape and synthesis of the archaellum.
Xing Ye   +2 more
doaj   +2 more sources

Autophosphorylation of the KaiC‐like protein ArlH inhibits oligomerization and interaction with ArlI, the motor ATPase of the archaellum

open access: yesMolecular Microbiology, Volume 116, Issue 3, Page 943-956, September 2021., 2021
KaiC is the central component in the regulation of the cyanobacterial circadian rhythm. KaiC‐like proteins are widespread in archaea, where they are thought to have originated and thought to perform diverse functions. We show that the KaiC‐like protein ArlH—an essential protein for archaeal motility—possesses autophosphorylation activity which mediates
J. Nuno de Sousa Machado   +7 more
wiley   +1 more source

Whole‐genome comparison between the type strain of Halobacterium salinarum (DSM 3754T) and the laboratory strains R1 and NRC‐1

open access: yesMicrobiologyOpen, Volume 9, Issue 2, February 2020., 2020
The genome of the Halobacterium salinarum type strain (91‐R6, DSM 3754) was compared at the DNA and protein levels to the genomes of two well‐studied laboratory strains, NRC‐1 and R1. The chromosomes and portions of the plasmids were very closely related. However, distinct homologs for proteins involved in motility and N‐glycosylation were encountered.
Friedhelm Pfeiffer   +4 more
wiley   +1 more source

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