@article{ZhouZhangGuietal.2015, author = {Zhou, Ying and Zhang, Ling and Gui, Jiadong and Dong, Fang and Cheng, Sihua and Mei, Xin and Zhang, Linyun and Li, Yongqing and Su, Xinguo and Baldermann, Susanne and Watanabe, Naoharu and Yang, Ziyin}, title = {Molecular Cloning and Characterization of a Short-Chain Dehydrogenase Showing Activity with Volatile Compounds Isolated from Camellia sinensis}, series = {Plant molecular biology reporter}, volume = {33}, journal = {Plant molecular biology reporter}, number = {2}, publisher = {Springer}, address = {New York}, issn = {0735-9640}, doi = {10.1007/s11105-014-0751-z}, pages = {253 -- 263}, year = {2015}, abstract = {Camellia sinensis synthesizes and emits a large variety of volatile phenylpropanoids and benzenoids (VPB). To investigate the enzymes involved in the formation of these VPB compounds, a new C. sinensis short-chain dehydrogenase/reductase (CsSDR) was isolated, cloned, sequenced, and functionally characterized. The complete open reading frame of CsSDR contains 996 nucleotides with a calculated protein molecular mass of 34.5 kDa. The CsSDR recombinant protein produced in Escherichia coli exhibited dehydrogenase-reductase activity towards several major VPB compounds in C. sinensis flowers with a strong preference for NADP/NADPH co-factors, and showed affinity for (R)/(S)-1-phenylethanol (1PE), phenylacetaldehyde, benzaldehyde, and benzyl alcohol, and no affinity for acetophenone (AP) and 2-phenylethanol. CsSDR showed the highest catalytic efficiency towards (R)/(S)-1PE. Furthermore, the transient expression analysis in Nicotiana benthamiana plants validated that CsSDR could convert 1PE to AP in plants. CsSDR transcript level was not significantly affected by floral development and some jasmonic acid-related environmental stress, and CsSDR transcript accumulation was detected in most floral tissues such as receptacle and anther, which were main storage locations of VPB compounds. Our results indicate that CsSDR is expressed in C. sinensis flowers and is likely to contribute to a number of floral VPB compounds including the 1PE derivative AP.}, language = {en} } @article{ZhouZengFuetal.2016, author = {Zhou, Ying and Zeng, Lanting and Fu, Xiumin and Mei, Xin and Cheng, Sihua and Liao, Yinyin and Deng, Rufang and Xu, Xinlan and Jiang, Yueming and Duan, Xuewu and Baldermann, Susanne and Yang, Ziyin}, title = {The sphingolipid biosynthetic enzyme Sphingolipid delta8 desaturase is important for chilling resistance of tomato}, series = {Scientific reports}, volume = {6}, journal = {Scientific reports}, publisher = {Nature Publ. Group}, address = {London}, issn = {2045-2322}, doi = {10.1038/srep38742}, pages = {10}, year = {2016}, abstract = {The physiological functions of sphingolipids in animals have been intensively studied, while less attention has been paid to their roles in plants. Here, we reveal the involvement of sphingolipid delta8 desaturase (SlSLD) in the chilling resistance of tomato (Solanum lycopersicum cv. Micro-Tom). We used the virus-induced gene silencing (VIGS) approach to knock-down SlSLD expression in tomato leaves, and then evaluated chilling resistance. Changes in leaf cell structure under a chilling treatment were observed by transmission electron microscopy. In control plants, SlSLD was highly expressed in the fruit and leaves in response to a chilling treatment. The degree of chilling damage was greater in SlSLD-silenced plants than in control plants, indicating that SlSLD knock-down significantly reduced the chilling resistance of tomato. Compared with control plants, SlSLD-silenced plants showed higher relative electrolytic leakage and malondialdehyde content, and lower superoxide dismutase and peroxidase activities after a chilling treatment. Chilling severely damaged the chloroplasts in SlSLD-silenced plants, resulting in the disruption of chloroplast membranes, swelling of thylakoids, and reduced granal stacking. Together, these results show that SlSLD is crucial for chilling resistance in tomato.}, language = {en} }