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ABSTRACT: Apoplastic H2O2 effects on phenolic metabolism and gene expression in a Norway spruce lignin-forming cell culture

PROVIDER: PRJEB13079 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR1331750_1.fastq.gz	Fastqsanger.gz
	ERR1331750_2.fastq.gz	Fastqsanger.gz
	ERR1331760_1.fastq.gz	Fastqsanger.gz
	ERR1331760_2.fastq.gz	Fastqsanger.gz
	ERR1331751_1.fastq.gz	Fastqsanger.gz

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Proteomics of exovesicle-enriched fraction of Norway Spruce, non-EDTA-extracted samples

Project description:Exovesicle-enriched fraction was isolated from the culture medium of tissue-cultured cells of Norway spruce during extracellular lignin formation and when lignin formation was hindered by scavenging of H2O2 from the culture medium. Proteomic analysis was conducted to investigate the protein cargo of the exovesicles.

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Project description:Monolignol transport during lignification is a partially solved puzzle: both the mechanism(s) and the transported form of monolignols are unknown in developing xylem of trees. We tested a hypothesis of an active, plasma membrane (PM)-localized transport of monolignol monomers, dimers, and/or glucosidic forms with membrane vesicles prepared of developing xylem, phloem, and lignin-forming, tissue-cultured cells of Norway spruce (Picea abies L. Karst.), as well as of a control material, non-lignifying tobacco (Nicotiana tabacum L.) BY-2 cells. Xylem and BY-2 vesicles transported both coniferin and p-coumaryl alcohol glucoside, but inhibitor assays suggested this transport being over the tonoplast. Based on similar inhibitor assays, lignin-forming, tissue42 cultured cells of spruce had coniferin transport putatively localizing on PM. Liquid chromatography-mass spectrometry (LC-MS/MS) analysis of membrane proteins isolated from spruce developing xylem, phloem and tissue-cultured cells revealed multiple transporters. These were compared to a transporter gene set that was gained by a correlation analysis with a selected set of spruce monolignol biosynthesis genes. Biochemical membrane vesicle assays showed no support for the ABC-transporter-mediated monolignol transport but point to secondary active transporters (such as MFS- or MATE-transporters). In contrast, proteomic and co-expression analyses suggest a role for ABC-transporters and MFS-transporters.

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