Hunting monolignol transporters: membrane proteomics and biochemical transport assays with membrane vesicles of Norway spruce

Author:

Väisänen Enni12,Takahashi Junko13ORCID,Obudulu Ogonna34ORCID,Bygdell Joakim5ORCID,Karhunen Pirkko6,Blokhina Olga1ORCID,Laitinen Teresa2,Teeri Teemu H2ORCID,Wingsle Gunnar3ORCID,Fagerstedt Kurt V1ORCID,Kärkönen Anna27ORCID

Affiliation:

1. Viikki Plant Science Centre, Organismal and Evolutionary Biology Research Programme, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland

2. Viikki Plant Science Centre, Department of Agricultural Sciences, University of Helsinki, Helsinki, Finland

3. Department of Forest Genetics and Plant Physiology, Umeå Plant Science Centre (UPSC), Swedish University of Agricultural Sciences, Umeå, Sweden

4. Department of Microbiology and Immunology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden

5. Department of Chemistry, Computational Life Science Cluster (CLiC), Umeå University, Umeå, Sweden

6. Department of Chemistry, University of Helsinki, Helsinki, Finland

7. Natural Resources Institute Finland (Luke), Production Systems, Plant Genetics, Helsinki, Finland

Abstract

Abstract Both the mechanisms of monolignol transport and the transported form of monolignols in developing xylem of trees are unknown. We tested the hypothesis of an active, plasma membrane-localized transport of monolignol monomers, dimers, and/or glucosidic forms with membrane vesicles prepared from developing xylem and lignin-forming tissue-cultured cells of Norway spruce (Picea abies L. Karst.), as well as from control materials, comprising non-lignifying Norway spruce phloem and tobacco (Nicotiana tabacum L.) BY-2 cells. Xylem and BY-2 vesicles transported both coniferin and p-coumaryl alcohol glucoside, but inhibitor assays suggested that this transport was through the tonoplast. Membrane vesicles prepared from lignin-forming spruce cells showed coniferin transport, but the Km value for coniferin was much higher than those of xylem and BY-2 cells. Liquid chromatography-mass spectrometry analysis of membrane proteins isolated from spruce developing xylem, phloem, and lignin-forming cultured cells revealed multiple transporters. These were compared with a transporter gene set obtained by a correlation analysis with a selected set of spruce monolignol biosynthesis genes. Biochemical membrane vesicle assays showed no support for ABC-transporter-mediated monolignol transport but point to a role for secondary active transporters (such as MFS or MATE transporters). In contrast, proteomic and co-expression analyses suggested a role for ABC transporters and MFS transporters.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Physiology

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