AbstractA short helix in the centre of the SecY subunit serves as a ‘plug’ blocking the protein channel. This site must be vacated if the channel is to open and accommodate translocating protein. We have synthesised a peptide mimic of this plug, and show that it binds to E. coli SecYEG, identifying a distinct and peripheral binding site. We propose that during active translocation the plug moves to this second discrete site and chart its position. Deletion of the plug in SecY increases the stoichiometry of the peptide–SecYEG interaction by also exposing the location it occupies in the channel. Binding of the plug peptide to the channel is unaffected by SecA
More than 30% of proteins synthesized in the cytoplasm of cells, must be transported into or across ...
Hydrophobic signal sequences target secretory polypeptides to a protein-conducting channel formed by...
Sec translocon is the major machinery for protein translocation in E.coli including SecYEG, SecA and...
AbstractA short helix in the centre of the SecY subunit serves as a ‘plug’ blocking the protein chan...
The SecYEG complex forms a protein-conducting channel in the inner membrane of Escherichia coli to s...
International audienceProtein translocation occurs across the energy-conserving bacterial membrane a...
The central pore of the SecYEG preprotein-conducting channel is closed at the periplasmic face of th...
SummaryThe Sec complex forms the core of a conserved machinery coordinating the passage of proteins ...
SummaryMany proteins are translocated across the bacterial plasma membrane by the interplay of the c...
AbstractSecYEG functions as a membrane channel for protein export. SecY constitutes the protein-cond...
During their biosynthesis, many proteins pass through the membrane via a hydrophilic channel formed ...
An important step in the biosynthesis of many proteins is their partial or complete translocation ac...
The transport of proteins across the plasma membrane in bacteria requires a channel formed from the ...
The SecYEG translocon of Escherichia coli mediates the translocation of preproteins across the cytop...
SummaryThe Sec translocon performs protein secretion and membrane protein insertion at the plasma me...
More than 30% of proteins synthesized in the cytoplasm of cells, must be transported into or across ...
Hydrophobic signal sequences target secretory polypeptides to a protein-conducting channel formed by...
Sec translocon is the major machinery for protein translocation in E.coli including SecYEG, SecA and...
AbstractA short helix in the centre of the SecY subunit serves as a ‘plug’ blocking the protein chan...
The SecYEG complex forms a protein-conducting channel in the inner membrane of Escherichia coli to s...
International audienceProtein translocation occurs across the energy-conserving bacterial membrane a...
The central pore of the SecYEG preprotein-conducting channel is closed at the periplasmic face of th...
SummaryThe Sec complex forms the core of a conserved machinery coordinating the passage of proteins ...
SummaryMany proteins are translocated across the bacterial plasma membrane by the interplay of the c...
AbstractSecYEG functions as a membrane channel for protein export. SecY constitutes the protein-cond...
During their biosynthesis, many proteins pass through the membrane via a hydrophilic channel formed ...
An important step in the biosynthesis of many proteins is their partial or complete translocation ac...
The transport of proteins across the plasma membrane in bacteria requires a channel formed from the ...
The SecYEG translocon of Escherichia coli mediates the translocation of preproteins across the cytop...
SummaryThe Sec translocon performs protein secretion and membrane protein insertion at the plasma me...
More than 30% of proteins synthesized in the cytoplasm of cells, must be transported into or across ...
Hydrophobic signal sequences target secretory polypeptides to a protein-conducting channel formed by...
Sec translocon is the major machinery for protein translocation in E.coli including SecYEG, SecA and...