KMID : 0624620110440110719
|
|
BMB Reports 2011 Volume.44 No. 11 p.719 ~ p.724
|
|
Molecular cloning and sequence and 3D models analysis of the Sec61¥á subunit of protein translocation complex from Penicillium ochrochloron
|
|
Azad Abul Kalam
Jahan Md. Asraful Hasan Md. Mahbub Ishikawa Takahiro Sawa Yoshihiro Shibata Hitoshi
|
|
Abstract
|
|
|
The Sec61¥á 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¥á subunit from Penicillium ochrochloron (PoSec61¥á). Sequence and 3D structural model analysis showed that PoSec61¥á conserved the typical characteristics of eukaryotic and prokaryotic Sec61¥á 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 ¥á-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¥á subunit homologues in archaea or other eukaryotes, respectively. Results reported herein indicate that the pore ring residues differ among Sec61¥á subunit homologues and two hydrophobic residues in the TM7 contribute to the pore ring formation.
|
|
KEYWORD
|
|
Pore aperture, Pore ring, PoSec61¥á, Sec61¥á subunit homologues, 3D models
|
|
FullTexts / Linksout information
|
|
|
|
Listed journal information
|
|
|