TY  - JOUR
A1  - Zhou, Ying
A1  - Zhang, Ling
A1  - Gui, Jiadong
A1  - Dong, Fang
A1  - Cheng, Sihua
A1  - Mei, Xin
A1  - Zhang, Linyun
A1  - Li, Yongqing
A1  - Su, Xinguo
A1  - Baldermann, Susanne
A1  - Watanabe, Naoharu
A1  - Yang, Ziyin
T1  - Molecular Cloning and Characterization of a Short-Chain Dehydrogenase Showing Activity with Volatile Compounds Isolated from Camellia sinensis
JF  - Plant molecular biology reporter
N2  - 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.
KW  - Camellia sinensis
KW  - 1-Phenylethanol
KW  - Phenylpropanoids
KW  - Short chain dehydrogenase
KW  - Volatile compound
Y1  - 2015
U6  - https://doi.org/10.1007/s11105-014-0751-z
SN  - 0735-9640
SN  - 1572-9818
VL  - 33
IS  - 2
SP  - 253
EP  - 263
PB  - Springer
CY  - New York
ER  - 
TY  - JOUR
A1  - Zhou, Ying
A1  - Zeng, Lanting
A1  - Fu, Xiumin
A1  - Mei, Xin
A1  - Cheng, Sihua
A1  - Liao, Yinyin
A1  - Deng, Rufang
A1  - Xu, Xinlan
A1  - Jiang, Yueming
A1  - Duan, Xuewu
A1  - Baldermann, Susanne
A1  - Yang, Ziyin
T1  - The sphingolipid biosynthetic enzyme Sphingolipid delta8 desaturase is important for chilling resistance of tomato
JF  - Scientific reports
N2  - 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.
Y1  - 2016
U6  - https://doi.org/10.1038/srep38742
SN  - 2045-2322
VL  - 6
PB  - Nature Publ. Group
CY  - London
ER  -