Molecular Characterization and Phylogenetic Analysis of the Eukaryotic Translation Initiation Factor 4A Gene in Antheraea pernyi (Lipdoptera: Saturniidae)

Abstract

Eukaryotic initiation factor 4A (eIF-4A) is an essential component for protein translation in eukaryotes. The eIF-4A gene ( ApeIF-4A ) was isolated and characterized from Antheraea pernyi (Guérin-Méneville) (Lepidoptera: Saturniidae). The obtained cDNA sequence was 1,435-bp long with an open reading frame of 1,266 bp encoding 421 amino acids. The predicted amino acid sequence shared several conserved features as found in known eIF-4As and revealed 74 and 78% identities with eIF-4As of Homo sapiens L. and Drosophila melanogaster (Meigen), respectively. Reverse transcription-polymerase chain reaction (RT-PCR) analysis showed that ApeIF-4A was transcribed at four developmental stages and in all tissues tested, suggesting that it plays an important role in development of A. pernyi . Homologous alignment suggested that eIF-4As are highly conserved throughout evolution of eukaryote organisms. Phylogenetic trees based on the amino acid and nucleotide sequences of eIF-4A demonstrated a similar topology with the classical systematics, suggesting that it has the potential value in phylogenetic inference of eukaryotes.

Identification and Characterization of a Novel Microvitellogenin from the Chinese Oak Silkworm Antheraea pernyi

“…The gene-specific primer pairs for mVg , Vg [ 20 ], and KK-42BP ( KK-42-binding protein ; [ 21 ]) are listed in Table 1 . The eIF-4A gene was used as an internal control [ 22 ]. We used the reverse transcription-polymerase chain reaction (RT-PCR) method to detect the expression pattern.…”

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

“…The results showed that A. pernyi eIF‐4A shares 82–99 % sequence identity with eIF‐5As in closely related species, and 72–73 % sequence identity with eIF‐5As in vertebrates. Sequence identity of >60 % indicates high conservation during the evolution of eukaryote organisms following divergence from a common ancestor (Embley & Martin ; Chen et al ). Furthermore, sequence alignment and prediction of functional domains revealed that the amino acid sequences of the conserved features of ApeIF‐5A, including the N‐terminal and C‐terminal domain, were even more highly conserved (Kapp & Lorsch ).…”