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Homo sapiens

ABSTRACT: Gene expression profiles of activin-A-induced human Tr1-like regulatory T cells and T conventional cells.

PROVIDER: PRJNA378523 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5320752.fastq.gz	Fastqsanger.gz
	SRR5320753.fastq.gz	Fastqsanger.gz
	SRR5320754.fastq.gz	Fastqsanger.gz
	SRR5320755.fastq.gz	Fastqsanger.gz

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Gene expression profiles of activin-A-induced human Tr1-like regulatory T cells and T conventional cells.

Project description:The aim of our studies was to investigate the molecular mechanisms underlying the differentiation of human Tr1-like regulatory T cells by the cytokine activin-A. We employed high-throughput sequencing of the whole T cell transcriptome and characterized the transcriptional profile of activin-A-induced human Tr1-like regulatory T cells (act-A-iTr1 cells) and compared it to those of Tconventional cells (Tconv). Our studies identified novel immunoregulatory molecules/pathways involved in the differentiation and effector function of human act-A-iTr1 cells.

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Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.

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