A rubber transferase activator is necessary for natural rubber biosynthesis in dandelion

Abstract

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. Natural rubber is composed of extremely long polymers of isoprene. In dandelion, a potential alternative source of latex for industry, a rubber transferase activator, homologous to the human Nogo-B receptor, is necessary for this synthesis.