High-molecular-mass natural rubber is a valuable plant-derived poly(cis-1,4-isoprene) with many industrial and medical applications. It is synthesized by a rubber cis-prenyltransferase (CPT) complex on the surface of rubber particles in specialized latex-producing cells known as laticifers. Here we show that Taraxacum brevicorniculatum rubber transferase activator (TbRTA), a dandelion homologue of the human Nogo-B receptor, is an essential component of the rubber transferase complex which interacts with rubber CPTs on the surface of rubber particles. The knockdown of TbRTA by RNA interference eliminated rubber biosynthesis, without affecting dolichol accumulation or protein glycosylation in the latex. We also found that TbRTA is localized on the endoplasmic reticulum membrane, supporting the current favoured model of rubber particle biogenesis. We therefore propose that TbRTA acts as a rubber CPT-binding protein that is necessary for the formation of an active rubber transferase complex
Summary 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.
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