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Background  Natural rubber is a biopolymer with exceptional qualities that cannot be completely replaced using synthetic alternatives. Although several key enzymes in the rubber biosynthetic pathway have been isolated, mainly from plants such as  Hevea brasiliensis ,  Ficus spec.  and the desert shrub  Parthenium argentatum , there have been no  in planta  functional studies, e.g. by RNA interference, due to the absence of efficient and reproducible protocols for genetic engineering. In contrast, the Russian dandelion  Taraxacum koksaghyz , which has long been considered as a potential alternative source of low-cost natural rubber, has a rapid life cycle and can be genetically transformed using a simple and reliable procedure. However, there is very little molecular data available for either the rubber polymer itself or its biosynthesis in  T. koksaghyz .    Results  We established a method for the purification of rubber particles - the active sites of rubber biosynthesis - from  T. koksaghyz  latex. Photon correlation spectroscopy and transmission electron microscopy revealed an average particle size of 320 nm, and  13 C nuclear magnetic resonance (NMR) spectroscopy confirmed that isolated rubber particles contain poly( cis -1,4-isoprene) with a purity >95%. Size exclusion chromatography indicated that the weight average molecular mass (    w) of  T. koksaghyz  natural rubber is 4,000-5,000 kDa. Rubber particles showed rubber transferase activity of 0.2 pmol min -1  mg -1 .  Ex vivo  rubber biosynthesis experiments resulted in a skewed unimodal distribution of [1- 14 C]isopentenyl pyrophosphate (IPP) incorporation at aw of 2,500 kDa. Characterization of recently isolated  cis -prenyltransferases (CPTs) from  T. koksaghyz  revealed that these enzymes are associated with rubber particles and are able to produce long-chain polyprenols in yeast.    Conclusions   T. koksaghyz  rubber particles are similar to those described for  H. brasiliensis . They contain very pure, high molecular mass poly( cis -1,4-isoprene) and the chain elongation process can be studied  ex vivo . Because of their localization on rubber particles and their activity in yeast, we propose that the recently described  T. koksaghyz  CPTs are the major rubber chain elongating enzymes in this species.  T. koksaghyz  is amenable to genetic analysis and modification, and therefore could be used as a model species for the investigation and comparison of rubber biosynthesis.

Characterization of rubber particles and rubber chain elongation in Taraxacum koksaghyz