Abstract
The steroidogenic acute regulatory protein (StAR) plays a key role in transferring cholesterol across the inner mitochondrial membrane. In this study, the StAR gene was isolated from the gonads of Clarias batrachus. The gene has an open reading frame of 857 bp and encodes 285 amino acids with a predicted molecular weight of 32 kDa. The signalP analysis predicted that StAR would be a non-secreted protein that lacks a signal peptide. The subcellular localization demonstrated that the presence of the StAR protein was higher in mitochondria (41.8%), followed by the nuclear region (37.1%) and cytoplasm (11.1%). The StAR protein was found to interact highly with cyp11a1, followed by the cytochrome P450 family 11 proteins and the START5 domain. The homology modelling revealed that the protein has 4 helices and twisted U-shaped 10 beta sheets numbered from αA to αD and β1 to β10, respectively. Molecular modelling analysis showed that resveratrol and eurycomanone has high binding affinity with the StAR protein. The C. batrachus StAR transcript was found to be expressed exclusively in the gonads, kidney, and liver. These results overall lay a solid foundation for understanding the structure of StAR protein in fish. The identification of 3D structures and binding sites will help in designing a structure-based drug of StAR agonists for the treatment of impaired steroidogenesis.
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