Journal ArticleDOI
Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily
TLDR
The Oxa1 superfamily performs membrane protein insertion in bacteria, the eukaryotic endoplasmic reticulum (ER), and endosymbiotic organelles as mentioned in this paper.Abstract:
Members of the Oxa1 superfamily perform membrane protein insertion in bacteria, the eukaryotic endoplasmic reticulum (ER), and endosymbiotic organelles. Here, we review recent structures of the three ER-resident insertases and discuss the extent to which structure and function are conserved with their bacterial counterpart YidC. Recent structures of eukaryotic membrane protein insertases of the Oxa1 superfamily reveal a conserved protein module and common mechanistic principles that enable membrane insertion of a diverse set of substrates.read more
Citations
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Journal ArticleDOI
The mechanisms of integral membrane protein biogenesis
TL;DR: In this article, the molecular basis of integral membrane protein targeting and insertion has been investigated, with tantalizing new insights into the poorly understood processes of multipass membrane protein biogenesis and multi-subunit protein complex assembly.
Journal ArticleDOI
The Dynamic SecYEG Translocon.
TL;DR: In this paper, the authors summarize the current knowledge about SecYEG-mediated protein transport, primarily in the model organism Escherichia coli, and describe the dynamic interaction of the SecYeg translocon with its multiple partner proteins.
Journal ArticleDOI
Membrane protein biogenesis at the ER: the highways and byways.
TL;DR: The Sec61 complex is the major protein translocation channel of the endoplasmic reticulum (ER), where it plays a central role in the biogenesis of membrane and secretory proteins.
Journal ArticleDOI
Capture and delivery of tail-anchored proteins to the endoplasmic reticulum.
TL;DR: In this paper, the authors review important new insights into the capture of nascent TA proteins at the ribosome by the GET pathway pretargeting complex and the mechanism of their delivery into the ER membrane by the Get receptor insertase.
Journal ArticleDOI
Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation.
TL;DR: In this paper, the authors follow the signal peptide into the endoplasmic reticulum (ER) and discuss the recent insights that structural biology has provided on the governing principles of those interactions.
References
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TL;DR: It is shown that membrane insertion of two Sec-independent proteins requires YidC, which is essential for E. coli viability and homologues are present in mitochondria and chloroplasts.
Journal ArticleDOI
The GET Complex Mediates Insertion of Tail-Anchored Proteins into the ER Membrane
Maya Schuldiner,Jutta Metz,Volker Schmid,Vladimir Denic,Magdalena Rakwalska,Hans Dieter Schmitt,Blanche Schwappach,Jonathan S. Weissman +7 more
TL;DR: It is shown that Get3, the yeast homolog of the TA-interacting factor Asna1/Trc40, specifically recognizes TMDs of TA proteins destined for the secretory pathway, which represents a key decision step, whose loss can lead to misinsertion ofTA proteins into mitochondria.
Journal ArticleDOI
Structural insight into the biogenesis of β-barrel membrane proteins
Nicholas Noinaj,Adam J. Kuszak,James C. Gumbart,Petra Lukacik,Hoshing Chang,Nicole C. Easley,Trevor Lithgow,Susan K. Buchanan +7 more
TL;DR: The structure of BamA is described, the central and essential component of the BAM complex, from two species of bacteria: Neisseria gonorrhoeae and Haemophilus ducreyi, which consists of a large periplasmic domain attached to a 16-strand transmembrane β-barrel domain.