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Methanocaldococcus jannaschii DSM 2661

ABSTRACT: Chromatin immunoprecipitation of Methanocaldococcus jannaschii transcription machinery

PROVIDER: PRJNA342581 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR4245580.fastq.gz	Fastqsanger.gz
	SRR4245590.fastq.gz	Fastqsanger.gz
	SRR4245581.fastq.gz	Fastqsanger.gz
	SRR4245591.fastq.gz	Fastqsanger.gz
	SRR4245582.fastq.gz	Fastqsanger.gz

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Methanocaldococcus jannaschii DSM 2661

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Effect of heat shock at 500 atm and pressure shock to 500 atm on Methanocaldococcus jannaschii

Project description:Growth and transcriptional profiles of the barophilic methanarchaeon Methanocaldococcus jannaschii were studied at temperatures up to 98C and pressures up to 500 atm. Application of 500 atm of hyperbaric pressure shifted the optimal growth temperature upwards, and heat shock from 88C to 98C at 500 atm resulted in termination of growth. Pressure shock of M. jannaschii from 7.8 to 500 atm over 15-min, the first pressure upshift reported for a barophile, did not accelerate growth. Transcriptional profiles indicated a similar pressure response under growth and heat shock at 500 atm and pressure shock to 500 atm suggesting that the commonly affected genes are important for high-pressure adaptation. Factorial microarray design allowed de-convolution of the interacting effect of elevated pressure and heat shock on expression profiles, thus suggesting genes that may contribute to the organism’s survival in the turbulent in situ conditions of deep-sea hydrothermal vents. Keywords: stress response, time course, high pressure, heat shock, pressure shock

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Cross-linking mass spectrometry and integrative modelling of Methanocaldococcus jannaschii GMP synthetase

Project description:GMP synthetases are enzymes that catalyze the conversion of XMP to GMP. The two-subunit type GMP synthetases are composed of a glutamine amidotransferase (GATase) subunit that catalyzes the conversion of Gln to Glu and ammonia, and the ATP pyrophosphatase (ATPPase) subunit that catalyzes the formation of AMP-XMP from ATP and XMP. The inactive GATase subunit is allosterically activated by the binding of substrates to the ATPPase subunit. Upon activation, the GATase subunit binds Gln and hydrolyzes it producing ammonia which is tunnelled to the ATPPase subunit. The two subunits form a tight complex to enable domain crosstalk. However, the Methanocaldococcus jannaschii GMP synthetase (MjGMPS) is unique as the GATase (MjGATase) and ATPPase (MjATPPase) subunits interact transiently. Here, we employed enzyme kinetics, X-ray crystallography, cross-linking mass spectrometry (XL-MS) and integrative modelling to understand the mechanistic basis for the various steps in the catalytic cycle of MjGMPS.

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MNase-seq analysis of the Methnocaldococcus jannaschii nucleoid reveals a general size-variable hypernucleosome architecture

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