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ABSTRACT: arabidopsis pyruvate kinase

PROVIDER: PRJNA1122224 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29352865_1.fastq.gz	Fastqsanger.gz
	SRR29352865_2.fastq.gz	Fastqsanger.gz
	SRR29352866_1.fastq.gz	Fastqsanger.gz
	SRR29352866_2.fastq.gz	Fastqsanger.gz
	SRR29352867_1.fastq.gz	Fastqsanger.gz

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Project description:We have previously shown that in Arabidopsis the three enzymes of lower glycolysis phosphoglycerate mutase (PGAM), enolase and pyruvate kinase form a complex which play an important role in co-sub-cellar localization the mitochondria to the chloroplast. Given that their metabolites of these mutants, the complementation of pgam mutant and overexpression of PGAM are still unclear, here, we present the gas chromatography mass spectrometry-based metabolomics data and plant growth phenotypes of them. Compared with wild type, both sugar and amino acid are significantly changed at mutants of phosphoglycerate mutase, enolase, pyruvate kinase. Overexpression the PGAM could decrease the content of 3PGA, sugar and several amino acids and increase the content of alanine and pyruvate. In addition, pgam mutant could not be fully complemented by nuclear sub-localized, the side-directed-mutated and the E.coli PGAM at plant phenotype and metabolites profiling, especially the content of 3PGA, serine and intermediates of TCA cycle. These data suggested that the low glycolysis complex play an important role at both mitochondria-chloroplast co-subcellar localization and the metabolites exchange.

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