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Transcriptional profiling of a NAGA kinase (nag5) mutant in Yarrowia lipolyitica

ABSTRACT: Transcriptional profiling of a NAGA kinase (nag5) mutant in Yarrowia lipolyitica

PROVIDER: PRJNA744548 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15065641.fastq.gz	Fastqsanger.gz
	SRR15065642.fastq.gz	Fastqsanger.gz
	SRR15065643.fastq.gz	Fastqsanger.gz
	SRR15065644.fastq.gz	Fastqsanger.gz
	SRR15065645.fastq.gz	Fastqsanger.gz

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Transcriptional profiling of a NAGA kinase (nag5) mutant in Yarrowia lipolyitica

Project description:In the fungus Yarrowia lipolytica the transcription of the genes encoding the enzymes of the N-acetylgucosamine (NAGA) pathway (NAG genes) is regulated by the presence of NAGA in the culture medium. In a wild-type strain, those genes are expressed at a very low level during growth in glucose while their expression increases 20 to 40 fold in cultures grown in NAGA. However, a deletion of the gene YlNAG5, encoding the NAGA kinase, abolishes this regulation and renders the transcription of those genes independent of the presence of NAGA in the medium (Flores and Gancedo 2015). A possibility to explain this result is that the protein Nag5 is a moonlighting protein with two functions: one as a metabolic kinase, the other as a regulator implicated in the control of the expression of the genes of the NAGA catabolic pathway. An alternative explanation would be that the transcriptional deregulation of the NAG genes in the mutant is triggered by an intracellular NAGA accumulation derived from chitin turnover. Our objective in this work was to decide between these two possibilities. To this end we studied the regulation of the expression of the NAG genes in a double mutant Ylnag5 ngt1 that cannot internalize NAGA and in a Ylnag5 mutant expressing mutated versions of YlNag5 or heterologous NAGA kinases. Additionally, we performed RNA-seq experiments to monitor the effects of the Ylnag5 mutation on the expression of genes not related to the NAGA pathway. Our results are consistent with the idea of NAGA kinase being a moonlighting protein with two roles, one as metabolic enzyme and other as regulatory protein in the transcription of some genes.

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