Results 21 to 30 of about 3,879 (192)

Endogenous SecA Catalyzes Preprotein Translocation at SecYEG [PDF]

Journal of Biological Chemistry, 1998
SecA is found in the cytosol and bound to the plasma membrane of Escherichia coli. Binding occurs either with high affinity at SecYEG or with low affinity to lipid. Domains of 65 and 30 kDa of SecYEG-bound SecA insert into the membrane upon interaction with preprotein and ATP.
J, Eichler, K, Rinard, W, Wickner
openaire   +2 more sources

Selectivity of the SecYEG Protein Translocation Channel [PDF]

Biophysical Journal, 2012
Many proteins are translocated across the endoplasmic reticulum membrane or the bacterial plasma membrane through a conserved channel, formed by a heterotrimeric protein complex (called the Sec61p complex in eukaryotes and the SecY complex in bacteria and archaea).
Knyazev, Denis, Lentz, Alexander, Pohl, Peter   +2 more
openaire   +3 more sources

Cellular dynamics of the SecA ATPase at the single molecule level

Scientific Reports, 2021
In bacteria, the SecA ATPase provides the driving force for protein secretion via the SecYEG translocon. While the dynamic interplay between SecA and SecYEG in translocation is widely appreciated, it is not clear how SecA associates with the translocon ...
Anne-Bart Seinen, Dian Spakman, Antoine M. van Oijen, Arnold J. M. Driessen   +3 more
doaj   +1 more source

Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC. [PDF]

PLoS ONE, 2017
SecA is an essential protein in the major bacterial Sec-dependent translocation pathways. E. coli SecA has 901 aminoacyl residues which form multi-functional domains that interact with various ligands to impart function. In this study, we constructed and
Ying-Hsin Hsieh, Ying-Ju Huang, Hao Zhang, Qian Liu, Yang Lu, Hsiuchin Yang, John Houghton, Chun Jiang, Sen-Fang Sui, Phang C Tai   +9 more
doaj   +1 more source

Driving Forces of Translocation Through Bacterial Translocon SecYEG [PDF]

The Journal of Membrane Biology, 2018
This review focusses on the energetics of protein translocation via the Sec translocation machinery. First we complement structural data about SecYEG's conformational rearrangements by insight obtained from functional assays. These include measurements of SecYEG permeability that allow assessment of channel gating by ligand binding and membrane voltage.
Denis G. Knyazev, Roland Kuttner, Mirjam Zimmermann, Ekaterina Sobakinskaya, Peter Pohl   +4 more
openaire   +3 more sources

Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins

Scientific Reports, 2021
The membrane insertase YidC inserts newly synthesized proteins by its hydrophobic slide consisting of the two transmembrane (TM) segments TM3 and TM5. Mutations in this part of the protein affect the insertion of the client proteins.
Anja Steudle, Dirk Spann, Eva Pross, Sri Karthika Shanmugam, Ross E. Dalbey, Andreas Kuhn   +5 more
doaj   +1 more source

The Bacterial Translocon SecYEG Opens upon Ribosome Binding [PDF]

Journal of Biological Chemistry, 2013
In co-translational translocation, the ribosome funnel and the channel of the protein translocation complex SecYEG are aligned. For the nascent chain to enter the channel immediately after synthesis, a yet unidentified signal triggers displacement of the SecYEG sealing plug from the pore.
Knyazev, Denis G., Lents, Alexander, Krause, Eberhard, Ollinger, Nicole, Siligan, Christine, Papinski, Daniel, Winter, Lukas, Horner, Andreas, Pohl, Peter   +8 more
openaire   +3 more sources

SecA-Mediated Protein Translocation through the SecYEG Channel [PDF]

Microbiology Spectrum, 2019
ABSTRACT In bacteria, the Sec translocase mediates the translocation of proteins into and across the cytoplasmic membrane. It consists of a protein conducting channel SecYEG, the ATP-dependent motor SecA, and the accessory SecDF complex. Here we discuss the function and structure of the Sec translocase.
Komarudin, Amalina Ghaisani, Driessen, Arnold J M   +1 more
openaire   +3 more sources

Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State

Cell Reports, 2015
The bacterial SecYEG translocon functions as a conserved protein-conducting channel. Conformational transitions of SecYEG allow protein translocation across the membrane without perturbation of membrane permeability.
Yoshiki Tanaka, Yasunori Sugano, Mizuki Takemoto, Takaharu Mori, Arata Furukawa, Tsukasa Kusakizako, Kaoru Kumazaki, Ayako Kashima, Ryuichiro Ishitani, Yuji Sugita, Osamu Nureki, Tomoya Tsukazaki   +11 more
doaj   +1 more source

Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex [PDF]

, 2012
The bacterial ATPase SecA and protein channel complex SecYEG form the core of an essential protein translocation machinery. The nature of the conformational changes induced by each stage of the hydrolytic cycle of ATP and how they are coupled to protein ...
Alice Robson, Bauer, Berger, Bessonneau, Breyton, Brundage, Cannon, Dalal, Deville, Ding, Duong, Egea, Erlandson, Erlandson, Gelis, Gold, Gold, Gold, Hizlan, Hunt, Ian Collinson, Karamanou, Lill, Or, Osborne, Osborne, Park, Park, Piggot, Piggot, Richard B. Sessions, Robson, Robson, Robson, Sarah Whitehouse, Tam, Van den Berg, Vicki A.M. Gold, William J. Allen, Wolf, Woodbury, Zimmer, Zimmer   +42 more
core   +2 more sources