The rubber tree latex quantitative proteomics research has made new progress

[introduction] Gade chemical network hot Daily: recently, New progress has been made in quantitative proteomics research of rubber latex, Through the quantitative proteomics of DIGE and iTRAQ technology, Found that the modified level of ethylene stimulates the production of latex mainly depends on the protein after translation.

Recently, China Academy of Tropical Agricultural Sciences Biology Institute Dr. Wang Xuchu and his team to make important progress in Brazil rubber tree latex quantitative proteomics research, first revealed the posttranslational modification of proteins in ethylene promoted new regulation mechanism of natural rubber in the synthesis process, which provides a new theoretical foundation for the thorough understanding of natural rubber biosynthesis protein regulation Brazil mechanism and improve the yield of rubber tree latex.
It is understood, ethylene can significantly promote latex production, but the related gene has not been significantly induced, it has always been a mystery study on the mechanism of regulation of natural rubber biosynthesis in distress. Through the quantitative proteomics of DIGE and iTRAQ technology, the team found that the modified level of ethylene stimulates the production of latex mainly depends on the protein after translation.
The results of the study found that , ethylene in the regulation of latex yield stimulation mechanism mainly lies in three aspects: first, the ethylene stimulation can significantly promote the small rubber latex particles; secondly, ethylene significantly inhibited mainly with rubber particle aggregation process regulating protease expression, thereby inhibiting latex agglutination, prolong the time to promote the flow of glue, latex outflow, and improve the latex yield; thirdly, regulation of ethylene production of latex mainly at the protein level, rather than the molecular regulation of water flat, in this process, protein post-translational modification of specific phosphorylation is key to protein modification.
The study also found for the first time, REF and SRPP play a key role in protein isoforms in the rubber synthesis process is mainly occurred in the phosphorylation of serine residues. Based on this, the team first constructed the role model in the regulation of latex protein biosynthesis.

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