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Molecular characterization and expression pattern of tripartite motif protein 39 in Gallus gallus with a complete
Chunqing Pan1, Heng Zhao, Lin Shen
1College of Food Sciences, China Agricultural University, Beijing 100080, China; E-Mails: pcq201005@yahoo.com.cn (C.P.); shen5000@cau.edu.cn (L.S.).
Abstract:
Members of tripartite motif (TRIM) proteins in mammals play important roles in multiple cellular processes in the immune system. In the present study we have obtained the chicken TRIM39 with the insertion of a base A at position 1006 bp, compared to the sequence in the NCBI database (Accession No: NM 001006196), which made TRIM39 fulfill the TRIM rule of domain composition with both PRY, and SPRY domains. The open reading frame consisted of 1392 bp encoding 463 amino acid residues. The amino acid sequences of TRIM39 protein in mammals were highly similar (from 91.48% to 99.61%), while chicken TRIM39 had relatively low homology with mammals (from 29.2% to 39.59%). Real time RT-PCR indicated that the mRNA expression level of TRIM39 was the highest in spleen, with a lower expression in liver, brain, and lung, suggesting it might be an important protein participating in the immune system.
