Results 51 to 60 of about 3,879 (192)

Residue-by-residue analysis of cotranslational membrane protein integration in vivo

eLife, 2021
We follow the cotranslational biosynthesis of three multispanning Escherichia coli inner membrane proteins in vivo using high-resolution force profile analysis. The force profiles show that the nascent chain is subjected to rapidly varying pulling forces
Felix Nicolaus, Ane Metola, Daphne Mermans, Amanda Liljenström, Ajda Krč, Salmo Mohammed Abdullahi, Matthew Zimmer, Thomas F Miller III, Gunnar von Heijne   +8 more
doaj   +1 more source

Signal Recognition Particle: An Essential Protein-Targeting Machine [PDF]

, 2013
The signal recognition particle (SRP) and its receptor compose a universally conserved and essential cellular machinery that couples the synthesis of nascent proteins to their proper membrane localization. The past decade has witnessed an explosion in
Akopian, David, Shan, Shu-ou, Shen, Kuang, Zhang, Xin   +3 more
core   +1 more source

SecYEG gets grabby with new proteins [PDF]

Journal of Cell Biology, 2013
![Figure][1] The ribosome (dark gray) and the rest of the targeting complex are about to hand over a protein to SecYEG (blue). Akopian et al. show that the bacterial protein channel SecYEG—the homologue of eukaryotic Sec61—deforms its molecular partner to take custody of ...
openaire   +1 more source

Preprotein mature domains contain translocase targeting signals that are essential for secretion [PDF]

, 2017
Secretory proteins are only temporary cytoplasmic residents. They are typically synthesized as preproteins, carrying signal peptides N-terminally fused to their mature domains. In bacteria secretion largely occurs posttranslationally through the membrane-
Albert Konijnenberg, Alexandra Tsirigotaki, Anastassios Economou, Bauer, Beckwith, Beerten, Bieker, Blobel, Bradford, Chang, Charalampos G. Kalodimos, Chatzi, Chatzi, Chen, Cunningham, De Geyter, Derman, Dimmer, Frank Sobott, García De La Torre, Gelis, Gouridis, Gouridis, Gouridis, Grudnik, Guex, Hegde, Huang, Hunt, Karamanou, Katerina E. Chatzi, Larkin, Le Loir, Lecker, Lill, Lill, Marina Koukaki, Marios Frantzeskos Sardis, Martoglio, Michaelis, Mitchell, Nikaido, Nikolina Šoštarić, Orfanoudaki, Ortega, Papanikolau, Papanikou, Park, Reineke, Rhoads, Roos, Saio, Schierle, Schneider, Sengoku, Shu, Spyridoula Karamanou, Stoscheck, Testa, Tsirigotaki, Uversky, Wilkins, Wilkins, Zimmer, Zimmer   +64 more
core   +2 more sources

Structure of the SecY Complex Unlocked by a Preprotein Mimic

Cell Reports, 2012
The Sec complex forms the core of a conserved machinery coordinating the passage of proteins across or into biological membranes. The bacterial complex SecYEG interacts with the ATPase SecA or translating ribosomes to translocate secretory and membrane ...
Dilem Hizlan, Alice Robson, Sarah Whitehouse, Vicki A. Gold, Janet Vonck, Deryck Mills, Werner Kühlbrandt, Ian Collinson   +7 more
doaj   +1 more source

SecYEG Proteoliposomes Catalyze the Δϕ-Dependent Membrane Insertion of FtsQ [PDF]

Journal of Biological Chemistry, 2004
In Escherichia coli, the insertion of most inner membrane proteins is mediated by the Sec translocase. Ribosome-bound nascent chains of Sec-dependent inner membrane proteins are targeted to the SecYEG complex via the signal recognition particle pathway.
van der Laan, M., Nouwen, N., Driessen, A.J.M.   +2 more
openaire   +3 more sources

Single‐molecule analysis of dynamics and interactions of the SecYEG translocon [PDF]

The FEBS Journal, 2020
Protein translocation and insertion into the bacterial cytoplasmic membrane are the essential processes mediated by the Sec machinery. The core machinery is composed of the membrane‐embedded translocon SecYEG that interacts with the secretion‐dedicated ATPase SecA and translating ribosomes.
Sabrina Koch, Anne‐Bart Seinen, Michael Kamel, Daniel Kuckla, Cornelia Monzel, Alexej Kedrov, Arnold J.M. Driessen   +6 more
openaire   +2 more sources

Investigating the SecY plug movement at the SecYEG translocation channel [PDF]

The EMBO Journal, 2005
Protein translocation occurs across the energy-conserving bacterial membrane at the SecYEG channel. The crystal structure of the channel has revealed a possible mechanism for gating and opening. This study evaluates the plug hypothesis using cysteine crosslink experiments in combination with various allelic forms of the Sec complex.
Tam, Patrick, Maillard, Antoine P., Chan, Kenneth, Duong, Franck   +3 more
openaire   +2 more sources

Synchronized Real-time Measurement of Sec-mediated Protein Translocation

Bio-Protocol, 2021
The Sec translocon, consisting of a heterotrimeric transmembrane channel (SecYEG) and an associated ATPase (SecA), catalyzes the export of unfolded proteins from the cytosol in bacteria.
Riti Gupta, Dmitri Toptygin, Christian Kaiser   +2 more
doaj   +1 more source

Glass is a viable substrate for precision force microscopy of membrane proteins [PDF]

, 2015
Scientific Reports ; 5:12550 ; DOI: 10.1038/srep12550.Chada, N. et al. Glass is a Viable Substrate for Precision Force Microscopy of Membrane Proteins. Sci. Rep.
Chada, Nagaraju, King, Gavin M., Matin, Tina Rezaie, Randall, Linda L., Sanganna Gari, Raghavendar Reddy, Sigdel, Krishna P.   +5 more
core   +2 more sources