SecY-SecA fusion protein retains the ability to mediate protein transport. [PDF]
In bacteria, the membrane protein complex SecY/E/G and SecA ATPase are essential for protein translocation. About 30% of newly synthesized proteins in the cytosol are targeted to and translocated across the cytoplasmic membrane by the Sec factors ...
Yasunori Sugano +4 more
doaj +4 more sources
Ribosome profiling reveals multiple roles of SecA in cotranslational protein export
Using a combination of ribosome profiling methods, Zhu et al. investigate the principles governing the cotranslational interaction of SecA with nascent proteins and reveal a hierarchical organization of protein export pathways in bacteria.
Zikun Zhu, Shuai Wang, Shu-ou Shan
doaj +4 more sources
The molecular mechanism of cotranslational membrane protein recognition and targeting by SecA [PDF]
Cotranslational protein targeting is a conserved process for membrane protein biogenesis. In Escherichia coli, the essential ATPase SecA was found to cotranslationally target a subset of nascent membrane proteins to the SecYEG translocase at the plasma ...
Ban, Nenad +5 more
core +6 more sources
Dynamic nature of SecA and its associated proteins in Escherichia coli. [PDF]
Mechanical properties such as physical constraint and pushing of chromosomes are thought to be important for chromosome segregation in Escherichia coli and it could be mediated by a hypothetical molecular tether.
Shun eAdachi +4 more
doaj +3 more sources
The dynamic action of SecA during the initiation of protein translocation [PDF]
Biotechnology and Biological Sciences Research Council (BBSRC) [a doctoral training grant Ph.D. studentship to S.W. and project grant number BB/I008675/1] and the Wellcome Trust [project grant number 084452]
Alice Robson +30 more
core +6 more sources
SecA mediates cotranslational targeting and translocation of an inner membrane protein [PDF]
Protein targeting to the bacterial plasma membrane was generally thought to occur via two major pathways: cotranslational targeting by signal recognition particle (SRP) and posttranslational targeting by SecA and SecB.
Shan, Shu-ou, Wang, Shuai, Yang, Chien-I
core +5 more sources
SecA – a multidomain and multitask bacterial export protein
Most bacterial secretory proteins destined to the extracytoplasmic space are secreted posttranslationally by the Sec translocase. SecA, a key component of the Sec system, is the ATPase motor protein, directly responsible for transferring the preprotein across the cytoplasmic membrane.
Patrycja Ambroziak +2 more
+6 more sources
Structural basis of SecA-mediated protein translocation
Secretory proteins are cotranslationally or posttranslationally translocated across lipid membranes via a protein-conducting channel named SecY in prokaryotes and Sec61 in eukaryotes. The vast majority of secretory proteins in bacteria are driven through the channel posttranslationally by SecA, a highly conserved ATPase.
Linlin Dong +6 more
openaire +2 more sources
SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels [PDF]
Abstract Sec-dependent protein translocation is an essential process in bacteria. SecA is a key component of the translocation machinery and has multiple domains that interact with various ligands. SecA acts as an ATPase motor to drive the precursor protein/peptide through the SecYEG protein translocation channels.
Jinshan, Jin +7 more
openaire +2 more sources
Dimeric SecA is essential for protein translocation [PDF]
SecA facilitates bacterial protein translocation by its association with presecretory or membrane proteins and the SecYEG translocon channel. Once assembled, SecA ATPase undergoes cycles of membrane insertion and retraction at SecYEG that drive protein translocation in a stepwise fashion.
Lucia B, Jilaveanu +2 more
openaire +2 more sources

