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Transcriptomic profilings of bovine mammary epithelial cells stimulated by ten different essential amino acids

ABSTRACT: Transcriptomic profilings of bovine mammary epithelial cells stimulated by ten different essential amino acids

PROVIDER: PRJNA972772 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR24572900_1.fastq.gz	Fastqsanger.gz
	SRR24572900_2.fastq.gz	Fastqsanger.gz
	SRR24572901_1.fastq.gz	Fastqsanger.gz
	SRR24572901_2.fastq.gz	Fastqsanger.gz
	SRR24572902_1.fastq.gz	Fastqsanger.gz

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Transcriptomic profilings of bovine mammary epithelial cells stimulated by ten different essential amino acids

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Compilation of transcriptomics, non-targeted metabolomics and targeted metabolomics data in bovine mammary epithelial cells stimulated by ten different essential amino acids (Untargeted metabolomics)

Project description:Divergence in the non-targeted metabolite profilings of bovine mammary epithelial cells (BMECs) were systematically captured with regard to 10 individual essential amino acid (EAA) availability. BMECs cultured in 6-well plates were first serum-starved overnight and subsequently assigned to 1 of 12 treatment media (n = 6). DMEM-F12 medium is the positive control treatment (POS), while DMEM-F12 medium devoid of all EAA served as the negative control treatment (NEG). A total of 10 treatments were NEG individually supplemented with arginine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan or valine (Sigma-Aldrich, MO, USA). Individual EAA were supplemented to achieve concentrations equal to those of POS. After 6-h treatment, all cell samples were taken at the same time, frozen in liquid nitrogen and stored at -80 °C until required. Untargeted metabolomics is reported in the current study <a href='https://www.ebi.ac.uk/metabolights/MTBLS7789' rel='noopener noreferrer' target='_blank'>MTBLS7789</a>.Targeted metabolomics is reported in <a href='https://www.ebi.ac.uk/metabolights/MTBLS3956' rel='noopener noreferrer' target='_blank'>MTBLS3956</a>.

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Project description:Comparison of the proteins of thermophilic, mesophilic and psychrophilic prokaryotes has revealed a number of features characteristic to proteins adapted to high temperatures, which increase their thermostability. These characteristics include an excess of disulfide bonds, salt bridges, hydrogen bonds, and hydrophobic interactions, and a depletion in intrinsically disordered regions. It is unclear, however, whether such differences can also be observed when comparing proteins that are adapted to temperatures that are more subtly different. When an organism is exposed to high temperatures, a subset of its proteins are overexpressed (heat-induced proteins), whereas others are repressed (heat-repressed proteins). Here, we determine the expression levels of all Arabidopsis thaliana genes at 22 and 37°C, and compare the amino acid compositions and levels of intrinsic disorder of heat-induced and heat-repressed proteins. We show that heat-induced proteins are enriched in electrostatically charged amino acids and depleted in polar amino acids, mirroring thermopile proteins. However, in contrast with thermophile proteins, heat-repressed proteins are enriched in intrinsically disordered regions and depleted in hydrophobic amino acids. These results indicate that temperature adaptation at the level of amino acid composition and intrinsic disorder can be observed not only in proteins of thermophilic organisms, but also in eukaryotic heat-induced proteins; however, the underlying adaptation pathways are similar but not exactly the same.

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