Abstract
Membrane proteins require protein machineries to insert their hydrophobic transmembrane domains (TMDs) into the lipid bilayer. A functional analysis of protein insertases in this issue of PLOS Biology reveals that the fundamental mechanism of membrane protein insertion is universally conserved.
Highlights
The evolvement of complex eukaryotic cells was accompanied by the formation of subcompbio.3001558 partments surrounded by lipid bilayers
Gungor and colleagues uncovered that the ER membrane complex (EMC) core complex can functionally replace the mitochondrial insertase Oxa1, pointing toward the conservation of a fundamental mechanism despite an evolutionary separation of archaeal and bacterial lineages, which took place about 3 billion years ago
The compensation by mito-EMC is surprising in regard of the different lipid composition of endoplasmic reticulum (ER) and mitochondria and further supports membrane thinning as mechanism for transmembrane domain (TMD) insertion, which is mainly dependent on lipid chain length rather than overall lipid composition
Summary
The evolvement of complex eukaryotic cells was accompanied by the formation of subcompbio.3001558 partments surrounded by lipid bilayers. Ponents of the ER membrane complex (EMC) can functionally replace the mitochondrial Oxa1 insertase [8,9].
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