Uncovering mechanisms of rubber biosynthesis in Taraxacum koksaghyz - role of cis-prenyltransferase-like 1 protein.


Journal

The Plant journal : for cell and molecular biology
ISSN: 1365-313X
Titre abrégé: Plant J
Pays: England
ID NLM: 9207397

Informations de publication

Date de publication:
11 2019
Historique:
received: 06 10 2018
revised: 08 07 2019
accepted: 12 07 2019
pubmed: 26 7 2019
medline: 4 8 2020
entrez: 26 7 2019
Statut: ppublish

Résumé

The Russian dandelion Taraxacum koksaghyz synthesizes considerable amounts of high-molecular-weight rubber in its roots. The characterization of factors that participate in natural rubber biosynthesis is fundamental for the establishment of T. koksaghyz as a rubber crop. The cis-1,4-isoprene polymers are stored in rubber particles. Located at the particle surface, the rubber transferase complex, member of the cis-prenyltransferase (cisPT) enzyme family, catalyzes the elongation of the rubber chains. An active rubber transferase heteromer requires a cisPT subunit (CPT) as well as a CPT-like subunit (CPTL), of which T. koksaghyz has two homologous forms: TkCPTL1 and TkCPTL2, which potentially associate with the rubber transferase complex. Knockdown of TkCPTL1, which is predominantly expressed in latex, led to abolished poly(cis-1,4-isoprene) synthesis but unaffected dolichol content, whereas levels of triterpenes and inulin were elevated in roots. Analyses of latex from these TkCPTL1-RNAi plants revealed particles that were similar to native rubber particles regarding their particle size, phospholipid composition, and presence of small rubber particle proteins (SRPPs). We found that the particles encapsulated triterpenes in a phospholipid shell stabilized by SRPPs. Conversely, downregulating the low-expressed TkCPTL2 showed no altered phenotype, suggesting its protein function is redundant in T. koksaghyz. MS-based comparison of latex proteomes from TkCPTL1-RNAi plants and T. koksaghyz wild-types discovered putative factors that convert metabolites in biosynthetic pathways connected to isoprenoids or that synthesize components of the rubber particle shell.

Identifiants

pubmed: 31342578
doi: 10.1111/tpj.14471
doi:

Substances chimiques

Butadienes 0
Hemiterpenes 0
Latex 0
Plant Proteins 0
Proteome 0
Triterpenes 0
isoprene 0A62964IBU
Carbon 7440-44-0
Inulin 9005-80-5
Transferases EC 2.-
cis-prenyl transferase EC 2.5.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

591-609

Informations de copyright

© 2019 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd.

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Auteurs

Eva Niephaus (E)

Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Münster, Germany.

Boje Müller (B)

Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Münster, Germany.

Nicole van Deenen (N)

Institute of Plant Biology and Biotechnology, University of Münster, Münster, Germany.

Ines Lassowskat (I)

Institute of Plant Biology and Biotechnology, University of Münster, Münster, Germany.

Martin Bonin (M)

Institute of Plant Biology and Biotechnology, University of Münster, Münster, Germany.

Iris Finkemeier (I)

Institute of Plant Biology and Biotechnology, University of Münster, Münster, Germany.

Dirk Prüfer (D)

Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Münster, Germany.
Institute of Plant Biology and Biotechnology, University of Münster, Münster, Germany.

Christian Schulze Gronover (C)

Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Münster, Germany.

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