Biomedical subjects
Publications and source records attributed to Jan-Willem L de Gier.
The bacterium Escherichia coli is one of the most popular model systems to study the assembly of membrane proteins of the so-called helix-bundle class. Here, based on this system, we review and discuss what is currently known about the assembly of these membrane proteins. In addition, we will briefly review and discuss how E. coli has been used as a vehicle for the overexpression of membrane proteins.
In the bacterium Escherichia coli, inner membrane proteins (IMPs) are generally targeted through the signal recognition particle pathway to the Sec translocon, which is capable of both linear transport into the periplasm and lateral transport into the lipid bilayer. Lateral transport seems to be assisted by the IMP YidC. In this article, we discuss recent observations that point to a key role for the ribosome in IMP targeting and to the diverse roles of YidC in IMP assembly.
YidC was recently shown to play an important role in the assembly of inner membrane proteins (IMPs) both in conjunction with and separate from the Sec-translocon. Little is known about the biogenesis and structural and functional properties of YidC, itself a polytopic IMP. Here we analyze the targeting and membrane integration of YidC using in vivo and in vitro approaches. The combined data indicate that YidC is targeted by the signal recognition particle and inserts at the SecAYEG-YidC translocon early during biogenesis, unlike its mitochondrial homologue Oxa1p. In addition, YidC is shown to be relatively abundant compared with other components involved in IMP assembly and is predominantly localized at the poles of the cell.
Over recent years, much progress has been made in the identification and characterization of factors involved in the biosynthesis of integral membrane proteins of the helix-bundle type. In addition, our knowledge of membrane protein structure and the forces stabilizing helix-helix interactions in a lipid environment is expanding rapidly. However, it is still not clear how a membrane protein folds into its final form in vivo, nor what constraints there are on the folded structure that results from the mechanistic details of translocon-mediated assembly rather than simply from the thermodynamics of protein-lipid interactions.