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  • Công bố khoa học và công nghệ Việt Nam

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Phạm Ngọc Vinh, Hong Gil Nam, Nguyễn Huy Hoàng, Đỗ Thị Trinh(1)

Phân lập các protein tương tác với ADP-Glucose pyrophosphorylase nằm ngoài vùng lục lạp ở Arabidopsis thaliana

Identification of non plastidic ADP-glucose pyrophosphorylase unconventional partners in Arabidopsis thaliana

Sinh học

2014

4

522-528

0866-7160

ADP-glucose pyrophosphorylase (ATP: alpha-glucose-I-phosphate adenylyl transferase, ADGase) previously has been studied as a key regulatory enzyme in the starch biosynthetic pathway in plant. Surprisingly, ADP-glucose pyrophosphorylase small subunit APSI (ADGl) was found not only in chloroplast but also in non plastidic region, especially, small proportion in nucleus. To elucidate the novel mechanislDS underlying non plastidic ADGI actions, yeast two-hybrid screening was used to identify proteins associated with ADGl. Yeast two hybrid and co-immunoprecipitation (Co-IP) assay were used to confirm the interaction between ADGl and interacting candidates. Furthermore, localization of interacting proteins was analyzed using Green Fluorescent Protein (GFP) fusion proteins under laser scanning microscopy. Two protein RPC4 (RNA polymerase III subunit) and LSU3 (Response to low Sulfur 3) were confirmed as strong candidates that interact with ADGl. Therefore, the authors hypothesized that non plastidic localized ADGl might have additional function which mediates plant cellular metabolism status and intracellular signaling to regulate proper plant growth and development.

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