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The structure of the Sec complex and the problem of protein translocation
Author(s) -
Robson Alice,
Collinson Ian
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400832
Subject(s) - endoplasmic reticulum , sec61 , membrane protein , microbiology and biotechnology , cytosol , peripheral membrane protein , membrane contact site , transport protein , biology , membrane transport protein , integral membrane protein , translocon , archaea , biochemistry , membrane , gene , enzyme
Proteins synthesized in the cytosol either remain there or are localized to a specific membrane and subsequently translocated to another cellular compartment. These extracytosolic proteins have to cross, or be inserted into, a phospholipid bilayer—a process governed by membrane‐bound protein transporters designed to recognize and receive appropriate polypeptides and thread them through the membrane. One such translocation complex, SecY/Sec61, is found in every cell, in either the plasma membrane of bacteria and archaea or the endoplasmic reticulum membrane of eukaryotes. Recent structural findings, combined with previous genetic and biochemical studies, have helped to describe how the passage of proteins through the membrane might occur, but several points of uncertainty remain.