AbstractTranslocation of proteins through the inner membrane of E. coli is normally catalyzed by the so-called sec-machinery. Yet, many integral inner membrane proteins appear not to require a fully functional sec-machinery for proper insertion, in spite of the fact that sometimes quite sizable domains have to be translocated to the periplasmic side. This review will focus on recent studies of sec-independent translocation events in an attempt to pin-point the main differences between sec-dependent and sec-independent translocation
In bacteria, more than one-third of the proteins synthesized in the cell accomplish their function o...
AbstractMost integral membrane proteins, both in prokaryotic and eukaryotic cells, are co-translatio...
SummaryThe Sec complex forms the core of a conserved machinery coordinating the passage of proteins ...
AbstractTranslocation of proteins through the inner membrane of E. coli is normally catalyzed by the...
AbstractThe sec machinery catalyzes the translocation of nascent polypeptide chains across the inner...
AbstractWe describe a secretory E. coli protein with a novel phenotype: signal peptide cleavage is l...
AbstractThe protein translocation apparatus in Escherichia coli has been studied both genetically an...
A remarkable feature of proteins of the SecD and SecF family involved in protein translocation is th...
SecA undergoes conformational changes during translocation, inserting domains into and across the me...
AbstractThe molecular events of membrane translocation and insertion have been investigated using a ...
The Escherichia coli SecYEG complex forms a transmembrane channel for both protein export and membra...
The SecYEG complex forms a protein-conducting channel in the inner membrane of Escherichia coli to s...
AbstractThe Escherichia coli SecYEG complex forms a transmembrane channel for both protein export an...
SummaryMany proteins are translocated across the bacterial plasma membrane by the interplay of the c...
For a long time, it was generally assumed that the biogenesis of inner membrane proteins in Escheric...
In bacteria, more than one-third of the proteins synthesized in the cell accomplish their function o...
AbstractMost integral membrane proteins, both in prokaryotic and eukaryotic cells, are co-translatio...
SummaryThe Sec complex forms the core of a conserved machinery coordinating the passage of proteins ...
AbstractTranslocation of proteins through the inner membrane of E. coli is normally catalyzed by the...
AbstractThe sec machinery catalyzes the translocation of nascent polypeptide chains across the inner...
AbstractWe describe a secretory E. coli protein with a novel phenotype: signal peptide cleavage is l...
AbstractThe protein translocation apparatus in Escherichia coli has been studied both genetically an...
A remarkable feature of proteins of the SecD and SecF family involved in protein translocation is th...
SecA undergoes conformational changes during translocation, inserting domains into and across the me...
AbstractThe molecular events of membrane translocation and insertion have been investigated using a ...
The Escherichia coli SecYEG complex forms a transmembrane channel for both protein export and membra...
The SecYEG complex forms a protein-conducting channel in the inner membrane of Escherichia coli to s...
AbstractThe Escherichia coli SecYEG complex forms a transmembrane channel for both protein export an...
SummaryMany proteins are translocated across the bacterial plasma membrane by the interplay of the c...
For a long time, it was generally assumed that the biogenesis of inner membrane proteins in Escheric...
In bacteria, more than one-third of the proteins synthesized in the cell accomplish their function o...
AbstractMost integral membrane proteins, both in prokaryotic and eukaryotic cells, are co-translatio...
SummaryThe Sec complex forms the core of a conserved machinery coordinating the passage of proteins ...