Faculty Opinions recommendation of Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET Insertase Complex.

2020 ◽  
Author(s):  
Tom Rapoport ◽  
Navdar Sever
Keyword(s):  
Membrane Protein ◽  
Structural Basis ◽  
Protein Biogenesis

scholarly journals Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET Insertase Complex

2020 ◽  
Vol 80 (1) ◽  
pp. 72-86.e7 ◽  
Author(s):  
Melanie A. McDowell ◽  
Michael Heimes ◽  
Francesco Fiorentino ◽  
Shahid Mehmood ◽  
Ákos Farkas ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Structural Basis ◽  
Protein Biogenesis

scholarly journals Structural Basis for Tail-Anchored Membrane Protein Biogenesis by the Get3-Receptor Complex

Science ◽  
2011 ◽  
Vol 333 (6043) ◽  
pp. 758-762 ◽  
Author(s):  
S. Stefer ◽  
S. Reitz ◽  
F. Wang ◽  
K. Wild ◽  
Y.-Y. Pang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Structural Basis ◽  
Receptor Complex ◽  
Protein Biogenesis

scholarly journals Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p

2010 ◽  
Vol 29 (24) ◽  
pp. 4083-4093 ◽  
Author(s):  
Yasuhiko Sato ◽  
Hiroyuki Shibata ◽  
Toru Nakatsu ◽  
Hiroaki Nakano ◽  
Yoshinori Kashiwayama ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Structural Basis ◽  
Peroxisomal Membrane ◽  
Protein Carrier ◽  
Peroxisomal Membrane Protein

scholarly journals Energetics of side-chain snorkeling in transmembrane helices probed by nonproteinogenic amino acids

2016 ◽  
Vol 113 (38) ◽  
pp. 10559-10564 ◽  
Author(s):  
Karin Öjemalm ◽  
Takashi Higuchi ◽  
Patricia Lara ◽  
Erik Lindahl ◽  
Hiroaki Suga ◽  
...  
Keyword(s):  
Amino Acids ◽  
Membrane Protein ◽  
Side Chain ◽  
Transmembrane Helices ◽  
Transmembrane Segments ◽  
Charged Amino Acids ◽  
Protein Biogenesis ◽  
Quantitative Basis ◽  
Apparent Free Energy ◽  
Integration Efficiency

Cotranslational translocon-mediated insertion of membrane proteins into the endoplasmic reticulum is a key process in membrane protein biogenesis. Although the mechanism is understood in outline, quantitative data on the energetics of the process is scarce. Here, we have measured the effect on membrane integration efficiency of nonproteinogenic analogs of the positively charged amino acids arginine and lysine incorporated into model transmembrane segments. We provide estimates of the influence on the apparent free energy of membrane integration (ΔGapp) of “snorkeling” of charged amino acids toward the lipid–water interface, and of charge neutralization. We further determine the effect of fluorine atoms and backbone hydrogen bonds (H-bonds) on ΔGapp. These results help establish a quantitative basis for our understanding of membrane protein assembly in eukaryotic cells.

scholarly journals The ribosome receptors Mrx15 and Mba1 jointly organize cotranslational insertion and protein biogenesis in mitochondria

2018 ◽  
Vol 29 (20) ◽  
pp. 2386-2396 ◽  
Author(s):  
Braulio Vargas Möller-Hergt ◽  
Andreas Carlström ◽  
Katharina Stephan ◽  
Axel Imhof ◽  
Martin Ott
Keyword(s):  
Membrane Protein ◽  
Mitochondrial Gene ◽  
Ribosomal Subunit ◽  
Mitochondrial Translation ◽  
Protein Insertion ◽  
Mitochondrial Ribosomes ◽  
Protein Biogenesis ◽  
Membrane Bound ◽  
Highly Hydrophobic ◽  
Soluble C

Mitochondrial gene expression in Saccharomyces cerevisiae is responsible for the production of highly hydrophobic subunits of the oxidative phosphorylation system. Membrane insertion occurs cotranslationally on membrane-bound mitochondrial ribosomes. Here, by employing a systematic mass spectrometry–based approach, we discovered the previously uncharacterized membrane protein Mrx15 that interacts via a soluble C-terminal domain with the large ribosomal subunit. Mrx15 contacts mitochondrial translation products during their synthesis and plays, together with the ribosome receptor Mba1, an overlapping role in cotranslational protein insertion. Taken together, our data reveal how these ribosome receptors organize membrane protein biogenesis in mitochondria.

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