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Thermotoga maritima

ABSTRACT: Hyperthermophilic bacterium

PROVIDER: PRJNA35107 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	SRR1647690_1.fastq.gz	Fastqsanger.gz
	SRR1647690_2.fastq.gz	Fastqsanger.gz
	SRR1647700_1.fastq.gz	Fastqsanger.gz
	SRR1647700_2.fastq.gz	Fastqsanger.gz

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Thermotoga maritima transcription during exponential and stationary phase growth on 1 and 5 g/l yeast extract

Project description:Although proteins and peptides encoded in small open reading frames (ORFs < 100 AA) in microbial genomes can play critical roles as toxins, bacteriocins, transcriptional regulators, signaling molecules, and chaperones, many such ORFs remain annotated as “hypothetical proteins”. In the genome of the hyperthermophilic bacterium, Thermotoga maritima, nearly 2/3 of the 167 small ORFs have no known function. As a strategy for investigating the potential significance of specific small ORFs, growth conditions that could trigger the expression of genes encoding small ORFs were sought. A defined medium supplemented with either 1 or 5 g/L yeast extract was used to track transcriptional response during the transition from exponential to stationary phase.

2013-08-28 | GSE47072 | GEO

Thermotoga maritima MSB8

Project description:Hyperthermophilic organism that shows extensive horizontal gene transfer from archaea

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Thermotoga maritima transcription during exponential and stationary phase growth on 1 and 5 g/l yeast extract

Project description:Although proteins and peptides encoded in small open reading frames (ORFs < 100 AA) in microbial genomes can play critical roles as toxins, bacteriocins, transcriptional regulators, signaling molecules, and chaperones, many such ORFs remain annotated as M-bM-^@M-^\hypothetical proteinsM-bM-^@M-^]. In the genome of the hyperthermophilic bacterium, Thermotoga maritima, nearly 2/3 of the 167 small ORFs have no known function. As a strategy for investigating the potential significance of specific small ORFs, growth conditions that could trigger the expression of genes encoding small ORFs were sought. A defined medium supplemented with either 1 or 5 g/L yeast extract was used to track transcriptional response during the transition from exponential to stationary phase. RNA derived from exponential (1E) and stationary (1S) phase cultures grown on 1 g/l yeast extract was compared to RNA derived from exponential (5E) and stationary (5S) phase cultures grown on 5 g/l yeast extract using a four-slide loop design.

2013-08-28 | E-GEOD-47072 | biostudies-arrayexpress

Transcriptome analysis of Thermotoga maritima

Project description:This SuperSeries is composed of the SubSeries listed below.

2013-08-02 | GSE37483 | GEO

Dihydrodipicolinate synthase from Thermotoga maritima.

Project description:DHDPS (dihydrodipicolinate synthase) catalyses the branch point in lysine biosynthesis in bacteria and plants and is feedback inhibited by lysine. DHDPS from the thermophilic bacterium Thermotoga maritima shows a high level of heat and chemical stability. When incubated at 90 degrees C or in 8 M urea, the enzyme showed little or no loss of activity, unlike the Escherichia coli enzyme. The active site is very similar to that of the E. coli enzyme, and at mesophilic temperatures the two enzymes have similar kinetic constants. Like other forms of the enzyme, T. maritima DHDPS is a tetramer in solution, with a sedimentation coefficient of 7.2 S and molar mass of 133 kDa. However, the residues involved in the interface between different subunits in the tetramer differ from those of E. coli and include two cysteine residues poised to form a disulfide bond. Thus the increased heat and chemical stability of the T. maritima DHDPS enzyme is, at least in part, explained by an increased number of inter-subunit contacts. Unlike the plant or E. coli enzyme, the thermophilic DHDPS enzyme is not inhibited by (S)-lysine, suggesting that feedback control of the lysine biosynthetic pathway evolved later in the bacterial lineage.

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Transcriptome analysis of Thermotoga maritima

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2013-08-02 | E-GEOD-37483 | biostudies-arrayexpress

Thermotoga maritima

Project description:Thermotoga maritima Genome sequencing and assembly

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Thermotoga maritima

Project description:Thermotoga maritima transcription during exponential and stationary phase growth on 1 and 5 g/l yeast extract

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Thermotoga maritima wild type minimal media expression analysis

Project description:An eight chip study using total RNA recovered from separate wild-type cultures of Thermotoga maritima at mid-log with 3 different minimal sugar media.

2012-07-03 | GSE28822 | GEO

Thermotoga maritima NusG: domain interaction mediates autoinhibition and thermostability.

Project description:NusG, the only universally conserved transcription factor, comprises an N- and a C-terminal domain (NTD, CTD) that are flexibly connected and move independently in Escherichia coli and other organisms. In NusG from the hyperthermophilic bacterium Thermotoga maritima (tmNusG), however, NTD and CTD interact tightly. This closed state stabilizes the CTD, but masks the binding sites for the interaction partners Rho, NusE and RNA polymerase (RNAP), suggesting that tmNusG is autoinhibited. Furthermore, tmNusG and some other bacterial NusGs have an additional domain, DII, of unknown function. Here we demonstrate that tmNusG is indeed autoinhibited and that binding to RNAP may stabilize the open conformation. We identified two interdomain salt bridges as well as Phe336 as major determinants of the domain interaction. By successive weakening of this interaction we show that after domain dissociation tmNusG-CTD can bind to Rho and NusE, similar to the Escherichia coli NusG-CTD, indicating that these interactions are conserved in bacteria. Furthermore, we show that tmNusG-DII interacts with RNAP as well as nucleic acids with a clear preference for double stranded DNA. We suggest that tmNusG-DII supports tmNusG recruitment to the transcription elongation complex and stabilizes the tmNusG:RNAP complex, a necessary adaptation to high temperatures.

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