The C‐terminal cysteine of turbot Scophthalmus maximus translationally controlled tumour protein plays a key role in antioxidation and growth‐promoting functions

• Published in: Journal of Fish Biology
• Main Authors: Zhang, Z.‐X., Geng, D.‐Y., Han, Q., Liang, S.‐D., Guo, H.‐R.
• Other Authors: National Natural Science Foundation of China, Scholarship Foundation for Excellent Scientists of Shandong Province, Fundamental Research Funds for the Central Universities of China
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2013
• Subjects: Aquatic Science; Ecology, Evolution, Behavior and Systematics; Scophthalmus maximus; Turbot
• Online Access: http://dx.doi.org/10.1111/jfb.12231; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fjfb.12231; https://onlinelibrary.wiley.com/doi/pdf/10.1111/jfb.12231

The translationally controlled tumour protein (TCTP) of turbot Scophthalmus maximus ( SmTCTP ) contains only one cysteine (Cys 170 ) at the C‐terminal end. The biological role of this C‐terminal Cys 170 in the antioxidation and growth‐promoting functions of SmTCTP was examined by site‐directed mutation of C170A (Cys 170 →Ala 170 ). It was found that C170A mutation not only obviously decreased the antioxidation capacity of the mutant‐ smtctp ‐transformed bacteria exposed to 0·22 mM hydrogen peroxide, but also significantly interrupted the normal growth and survival of the mutant‐ smtctp ‐transformed bacteria and flounder Paralichthys olivaceus gill ( FG ) cells, indicating a key role played by Cys 170 in the antioxidation and growth‐promoting functions of SmTCTP . This study also suggested that the self‐dimerization or dimerization with other interacting proteins is critical to the growth‐promoting function of SmTCTP .