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Meiothermus ruber

ABSTRACT: Thermophilic bacterium

PROVIDER: PRJNA60931 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
		Other
	BAOR01.dat.gz	Other
	BAOR01.fasta.gz	Fasta.gz
	BAOR01.master.dat	Other
	JRGA01.dat.gz	Other

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Meiothermus silvanus

Project description:Thermophilic bacterium

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Meiothermus silvanus DSM 9946

Project description:Thermophilic bacterium

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Complete genome sequence of Meiothermus ruber type strain (21).

Project description:Meiothermus ruber (Loginova et al. 1984) Nobre et al. 1996 is the type species of the genus Meiothermus. This thermophilic genus is of special interest, as its members share relatively low degrees of 16S rRNA gene sequence similarity and constitute a separate evolutionary lineage from members of the genus Thermus, from which they can generally be distinguished by their slightly lower temperature optima. The temperature related split is in accordance with the chemotaxonomic feature of the polar lipids. M. ruber is a representative of the low-temperature group. This is the first completed genome sequence of the genus Meiothermus and only the third genome sequence to be published from a member of the family Thermaceae. The 3,097,457 bp long genome with its 3,052 protein-coding and 53 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.

| S-EPMC3035268 | biostudies-literature

Meiothermus ruber DSM 1279

Project description:Hot spring bacterium

| PRJNA28827 | ENA

Enhancement of membrane vesicle production by disrupting the degP gene in Meiothermus ruber H328.

Project description:The phenomenon of membrane vesicle (MV) production is known to be common to all bacterial cells. Although MVs are expected to be employed in a variety of applications, improving MV productivity is essential for applications. Since the deletion of the degP gene, a periplasmic dual-function protease and chaperone, in Escherichia coli has successfully improved MV production capacity, we tried to enhance MV productivity in the thermophilic M. ruber H328 by deleting the degP gene. One gene (mrH_0331) was selected for degP gene from the H328 genome and we constructed the mutant strain ∆degP by deleting the degP gene of the H328 strain that was replaced with the htk gene showing thermophilic kanamaycin resistance by homologous recombination. The mutant strain ∆degP exhibited smooth growth but a lower level of turbidity at 60 °C although there was no difference in growth at 55 °C between the wild strain and the mutant strain. Finally, we have confirmed that incubation at 60 °C increases MV in the mutant strain ∆degP strain about fivefold by using two fluorescent dyes, DiI and FM4-64, which is followed by TEM analysis. The deletion of the degP gene presumably causes an increase in denatured proteins at 60 °C, leading to enhanced MV production. Meanwhile, the S-layer protein included in the outer membrane of the H328 strain increased in the MV fraction prepared from the mutant cells incubated at 60 °C. This indicates that this method is effective for MV production and that degP deletion enhances it in strain H328.

| S-EPMC8674399 | biostudies-literature

Analysis of Thermosynechococcus elongatus BP1 response to co-cultivation with Meiothermus ruber strain A

Project description:The transcriptional response of the cyanobacteria T. elongatus to co-cultiavation with a heterotrophic partner M. ruber was examined under three varying light levels and three varying oxygen levels.

2017-01-27 | GSE94125 | GEO

Meiothermus ruber H328

Project description:Draft genome sequence of Meiothermus ruber H328 degrading chicken feathers.

| PRJDB858 | ENA

Draft Genome Sequence of Meiothermus ruber H328, Which Degrades Chicken Feathers, and Identification of Proteases and Peptidases Responsible for Degradation.

Project description:Meiothermus ruber H328 was isolated from Arima Hot Springs, Kobe, Japan, as a moderate thermophile. It has a strong ability to degrade intact chicken feathers. The enzymatic mechanism of the strain for feather degradation is unclear. The draft genome suggests potent enzyme candidates for degradation of keratin, a hard-to-degrade protein found in feathers.

| S-EPMC3642283 | biostudies-literature

Analysis of Thermosynechococcus elongatus BP1 and Meiothermus ruber strain A co-cultured under variable light and oxygen conditions

2017-01-20 | GSE93859 | GEO

Meiothermus ruber DSM 1279

Project description:Meiothermus ruber DSM 1279 Genome sequencing

| PRJNA196343 | ENA