Molecular cloning and expression analysis of the highly conserved eukaryotic translation initiation factor 5A (eIF‐5A) fromAntheraea pernyi

Eukaryotic initiation factor 5A (eIF‐5A) is a highly conserved protein found in all eukaryotic organisms that plays a key role in the regulation of many cellular processes including translation elongation, cell proliferation, programmed cell death, mRNA turnover and decay, and abiotic stress responses. In this study, the eIF‐5A gene from the Chinese oak silkwormAntheraea pernyi(Lepidoptera: Saturniidae) was characterized. The full‐lengthApeIF‐5AcDNA of 1056 bpincludes a 5′‐untranslated region (UTR) of 138 bp, a 3′‐UTR of 435 bp, and an open reading frame of 483 bpencoding a polypeptide of 160 amino acids. The deducedApeIF‐5Aprotein shares 99 %, 82 %, and 72 % sequence identity with orthologs inBombyx mori,Drosophila melanogasterandHomo sapiens, indicating high conservation during animal evolution. Real‐time quantitative reverse transcription PCR revealed expression in all four developmental stages and in all nine tissues tested, consistent with an important role in development. After challenge with lipopolysaccharide, the expression levels ofApeIF‐5Awere markedly upregulated. Phylogenetic analysis of amino acid sequences revealedA. pernyieIF‐5A was closely related toB. morieIF‐5A, consistent with traditional classification and other molecular data. The results indicate the potential value ofeIF‐5Ain phylogenetic analysis.