• 제목/요약/키워드: $Sec61{\alpha}$ subunit homologues

Search Result 2, Processing Time 0.015 seconds

Molecular cloning and sequence and 3D models analysis of the Sec61α subunit of protein translocation complex from Penicillium ochrochloron

  • Azad, Abul Kalam;Jahan, Md. Asraful;Hasan, Md. Mahbub;Ishikawa, Takahiro;Sawa, Yoshihiro;Shibata, Hitoshi
    • BMB Reports
    • /
    • v.44 no.11
    • /
    • pp.719-724
    • /
    • 2011
  • The $Sec61{\alpha}$ subunit is the core subunit of the protein conducting channel which is required for protein translocation in eukaryotes and prokaryotes. In this study, we cloned a $Sec61{\alpha}$ subunit from Penicillium ochrochloron ($PoSec61{\alpha}$). Sequence and 3D structural model analysis showed that $PoSec61{\alpha}$ conserved the typical characteristics of eukaryotic and prokaryotic $Sec61{\alpha}$ subunit homologues. The pore ring known as the constriction point of the channel is formed by seven hydrophobic amino acids. Two methionine residues from transmembrane ${\alpha}$-helice 7 (TM7) contribute to the pore ring formation and projected notably to the pore area and narrowed the pore compared with the superposed residues at the corresponding positions in the crystal structures or the 3D models of the $Sec61{\alpha}$ subunit homologues in archaea or other eukaryotes, respectively. Results reported herein indicate that the pore ring residues differ among $Sec61{\alpha}$ subunit homologues and two hydrophobic residues in the TM7 contribute to the pore ring formation.

Molecular Cloning of the Sec61p ${\gamma}$ Subunit Homologue Gene from the Mole Cricket, Gryllotalpa orientalis

  • Kim, Iksoo;Lee, Kwang-Sik;Jin, Byung-Rae;Kim, Eun-Sun;Lee, Heui-Sam;Ahn, Mi-Young;Sohn, Hung-Dae;Ryu, Kang-Sun
    • International Journal of Industrial Entomology and Biomaterials
    • /
    • v.5 no.1
    • /
    • pp.73-77
    • /
    • 2002
  • The Sec61 trimeric complex ($\alpha$,$\beta$, and ${\gamma}$ subunits) is one of the Sec-complex responsible for post-translational protein translocation across the endoplasmic reticulum membrane in diverse organisms. In this study, a cDNA encoding the Sec61p ${\gamma}$ subunit homologue was isolated from the cDNA library of the mole cricket, Gryllotalpa orientalis. Sequence analysis of a 442-bp cDNA clone showed it to contain an open reading frame of 68 amino acid residues consisted of 204-bp. The homologues of the gene were found in the GenBank database in a diverse organism including insect, mammals, fungi, and plants. The deduced amino acid sequence of Sec61p ${\gamma}$ subunit homologue of the mole cricket showed the highest homology to the gene of the singly known insect, Drosophila melanogester (93% identity), and the least homology to that of the baker's yeast, Saccharomyces cerevisiae (37.2%). Phylogenetic analysis also confirmed a close relationship between the insect Sec61p ${\gamma}$ subunit homologues of G. orientalis and D. melanogester. Hydropathy analysis of the cricket mole and published other data suggested that the hydrophobic segment close to C-terminus is predicted to be the putative membrane anchor, Multiple alignment of the Sec61p ${\gamma}$ subunit homologue among several organisms showed the presence of several conserved domains including the conserved proline at position 28.