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The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolism.

. 2018 Jan 22;15:7. eCollection 2018
Jing Tian 1 , Jiapan Liu 1 , Jieqiong Li 2 , Jingxin Zheng 3 , Lifang Chen 4 , Yujuan Wang 1 , Qiong Liu 1 , Jiazuan Ni 1
Jing Tian 1 , Jiapan Liu 1 , Jieqiong Li 2 , Jingxin Zheng 3 , Lifang Chen 4 , Yujuan Wang 1 , Qiong Liu 1 , Jiazuan Ni 1
+ et al

[No authors listed]

Author information
  • 1 1College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Marine Bioresources and Eco-environmental Science, Shenzhen University, Shenzhen, 518060 China.
  • 2 2College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060 China.
  • 3 3College of Life Sciences and Oceanography, Shenzhen Engineering Laboratory for Marine Algal Biotechnology, Shenzhen University, Shenzhen, 518060 China.
  • 4 4Department of Neurology, Shenzhen University 1st Affiliated Hospital, Shenzhen Second People's Hospital, Sungang West Road, Shenzhen, China.

摘要


Background:Selenoprotein F (SELENOF, was named as 15-kDa selenoprotein) has been reported to play important roles in oxidative stress, endoplasmic reticulum (ER) stress and carcinogenesis. However, the biological function of SELENOF is still unclear. Methods:A yeast two-hybrid system was used to screen the interactive protein of SELENOF in a human fetal brain cDNA library. The interaction between SELENOF and interactive protein was validated by fluorescence resonance energy transfer (FRET), co-immunoprecipitation (co-IP) and pull-down assays. The production of retinol was detected by high performance liquid chromatograph (HPLC). Results:Retinol dehydrogenase 11 (RDH11) was found to interact with SELENOF. RDH11 is an enzyme for the reduction of all-trans-retinaldehyde to all-trans-retinol (vitamin A). The production of retinol was decreased by SELENOF overexpression, resulting in more retinaldehyde. Conclusions:SELENOF interacts with RDH11 and blocks its enzyme activity to reduce all-trans-retinaldehyde.

KEYWORDS: Co-immunoprecipitation (co-IP), Fluorescence resonance energy transfer (FRET), Protein-protein interaction, Pull-down, Retinaldehyde, Retinol (vitamin a), Retinol dehydrogenase 11 (RDH11), SELENOF (Seleonoprotein F) , Yeast two hybrid system