Molecular Characterization, Bioinformatic Analysis, and Expression Profile of Lin-28 Gene and Its Protein from Arabian Camel (Camelus dromedarius)

Sultan N. Alharbi, Ibtehal S. Alduhaymi, Lama Alqahtani, Musaad A. Altammaami, Fahad M. Alhoshani, Deema K. Alrabiah, Saleh O. Alyemni, Khulud A. Alsulami, Waleed M. Alghamdi, Mohannad Fallatah
2019 International Journal of Molecular Sciences  
Lin-28 is an RNA-binding protein that is known for its role in promoting the pluripotency of stem cells. In the present study, Arabian camel Lin-28 (cLin-28) cDNA was identified and analyzed. Full length cLin-28 mRNA was obtained using the reverse transcription polymerase chain reaction (RT-PCR). It was shown to be 715 bp in length, and the open reading frame (ORF) encoded 205 amino acids. The molecular weight and theoretical isoelectric point (pI) of the cLin-28 protein were predicted to be
more » ... predicted to be 22.389 kDa and 8.50, respectively. Results from the bioinformatics analysis revealed that cLin-28 has two main domains: an N-terminal cold-shock domain (CSD) and a C-terminal pair of retroviral-type Cysteine3Histidine (CCHC) zinc fingers. Sequence similarity and phylogenetic analysis showed that the cLin-28 protein is grouped together Camelus bactrianus and Bos taurus. Quantitative real-time PCR (qPCR) analysis showed that cLin-28 mRNA is highly expressed in the lung, heart, liver, and esophageal tissues. Peptide mass fingerprint-mass spectrometry (PMF-MS) analysis of the purified cLin-28 protein confirmed the identity of this protein. Comparing the modeled 3D structure of cLin-28 protein with the available protein 3D structure of the human Lin-28 protein confirmed the presence of CSD and retroviral-type CCHC zinc fingers, and high similarities were noted between the two structures by using super secondary structure prediction.
doi:10.3390/ijms20092291 fatcat:enigzrn7cbd2hopnzxhlr65gd4