Results 61 to 70 of about 649 (118)

The Lrs14 family of DNA‐binding proteins as nucleoid‐associated proteins in the Crenarchaeal order Sulfolobales

open access: yesMolecular Microbiology, Volume 123, Issue 2, Page 132-142, February 2025.
Crenarchaeal Sulfolobales organize their genome with small, abundant nucleoid‐associated proteins. Here, we shed light on the distinct function of the Lrs14 family of aspecific DNA‐binding proteins, position these members toward the “chromatin organizing” side of the spectrum of DNA binders and propose a regulatory role for Lrs14s in global gene ...
Veerke De Kock   +2 more
wiley   +1 more source

Isolation and characterization of a novel methanogen Methanosarcina hadiensis sp. nov. from subsurface Boom Clay pore water

open access: yesEnvironmental Microbiology, Volume 26, Issue 12, December 2024.
We isolated a novel methanogenic archaeon, Methanosarcina hadiensis sp. nov. (TD41E1‐1), from Boom Clay pore water at a depth of 225 m. It exhibits unique characteristics compared to previously characterized Methanosarcina species, such as the inability to perform acetoclastic methanogenesis and the presence of extensive surface appendages.
Francisco Javier Giménez   +4 more
wiley   +1 more source

Transcriptomic evidence for an energetically advantageous relationship between Syntrophomonas wolfei and Methanothrix soehngenii

open access: yesEnvironmental Microbiology Reports, Volume 16, Issue 3, June 2024.
We studied predefined co‐cultures to investigate the influence of acetate scavenger Methanothrix soehngenii on butyrate oxidation by a co‐culture of Syntrophomonas wolfei and Methanospirillum hungatei. RNAseq was used to compare the gene expression profiles of syntroph S. wolfei with and without the presence of the acetate scavenger M.
Maaike S. Besteman   +2 more
wiley   +1 more source

FlaF is a [beta]-sandwich protein that anchors the archaellum in the archaeal cell envelope by binding the S-layer protein

open access: yes, 2015
SummaryArchaea employ the archaellum, a type IV pilus-like nanomachine, for swimming motility. In the crenarchaeon Sulfolobus acidocaldarius, the archaellum consists of seven proteins: FlaB/X/G/F/H/I/J.
Banerjee, Ankan   +7 more
core   +1 more source

Proposed Role for KaiC-Like ATPases as Major Signal Transduction Hubs in Archaea

open access: yesmBio, 2017
All organisms must adapt to ever-changing environmental conditions and accordingly have evolved diverse signal transduction systems. In bacteria, the most abundant networks are built around the two-component signal transduction systems that include ...
Kira S. Makarova   +2 more
doaj   +1 more source

A comprehensive history of motility and Archaellation in Archaea

open access: yes, 2021
Each of the three Domains of life, Eukarya, Bacteria and Archaea, have swimming structures that were all originally called flagella, despite the fact that none were evolutionarily related to either of the other two.
Sousa Machado, Joao Nuno de   +5 more
core   +1 more source

Archaeal membrane-associated proteases: insights on Haloferax volcanii and other haloarchaea

open access: yesFrontiers in Microbiology, 2015
The function of membrane proteases range from general house-keeping to regulation of cellular processes. Although the biological role of these enzymes in archaea is poorly understood, some of them are implicated in the biogenesis of the archaeal cell ...
Maria Ines Giménez   +2 more
doaj   +1 more source

Horizontal gene transfer of the functional archaellum machinery to bacteria

open access: yes
Motility in archaea is driven by a nanomachinery called the archaellum. So far archaella have been exclusively described for the archaeal domain, however, a recent study reported the presence of archaellum gene clusters in bacterial strains of the SAR202
TAIB, Najwa
core   +1 more source

The nucleotide-dependent interaction of FlaH and FlaI isessential for assembly and function of the archaellum motor

open access: yes, 2016
The motor of the membrane-anchored archaeal motility structure, the archaellum, contains FlaX, FlaI and FlaH. FlaX forms a 30 nm ring structure that acts as a scaffold protein and was shown to interact with the bifunctional ATPase FlaI and FlaH. However,
Albers, S.   +28 more
core   +1 more source

Data_Sheet_1_N-Glycosylation Is Important for Halobacterium salinarum Archaellin Expression, Archaellum Assembly and Cell Motility.docx

open access: yes, 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 (3826600)   +3 more
core   +1 more source

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