Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome
Bacteria execute a variety of protein transport systems for maintaining the proper composition of their different cellular compartments. The SecYEG translocon serves as primary transport channel and is engaged in transporting two different substrate ...
Lara Knüpffer +5 more
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Voltage Sensing in Bacterial Protein Translocation [PDF]
The bacterial channel SecYEG efficiently translocates both hydrophobic and hydrophilic proteins across the plasma membrane. Translocating polypeptide chains may dislodge the plug, a half helix that blocks the permeation of small molecules, from its ...
Bondar, Ana-Nicoleta +5 more
core +1 more source
Cross‐linked SecA dimers are not functional in protein translocation [PDF]
The ATPase SecA is involved in post‐translational protein translocation through the SecY channel across the bacterial inner membrane. SecA is a dimer that can dissociate into monomers with translocation activity. Here, we have addressed whether dissociation of the SecA dimer is required for translocation.
Or, Eran, Rapoport, Tom
openaire +2 more sources
Synchronized Real-time Measurement of Sec-mediated Protein Translocation
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 +2 more
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Unusual Metabolism and Hypervariation in the Genome of a Gracilibacterium (BD1-5) from an Oil-Degrading Community. [PDF]
The candidate phyla radiation (CPR) comprises a large monophyletic group of bacterial lineages known almost exclusively based on genomes obtained using cultivation-independent methods.
Andersen, Gary L +7 more
core +2 more sources
Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.
In prokaryotes, about one third of cellular proteins are translocated across the plasma membrane or inserted into it by concerted action of the cytoplasmic ATPase SecA and the universally conserved SecYEG heterotrimeric polypeptide-translocating pore ...
Alex Dajkovic +3 more
doaj +1 more source
SecA-mediated targeting and translocation of secretory proteins
More than 30 years of research have revealed that the dynamic nanomotor SecA is a central player in bacterial protein secretion. SecA associates with the SecYEG channel and transports polypeptides post-translationally to the trans side of the cytoplasmic membrane.
Katerina E. Chatzi +3 more
openaire +2 more sources
SecA protein is directly involved in protein secretion in Escherichia coli [PDF]
A high‐expression plasmid for the secA gene was constructed. The SecA protein was then overproduced in E. coli and purified. The purified SecA stimulated the in vitro translocation of a model secretory protein into inverted membrane vesicles pretreated with 4 M urea.
Kawasaki, Hisashi +4 more
openaire +2 more sources
Taming membranes: functional immobilization of biological membranes in hydrogels. [PDF]
Single molecule studies on membrane proteins embedded in their native environment are hampered by the intrinsic difficulty of immobilizing elastic and sensitive biological membranes without interfering with protein activity.
Ilja Kusters +5 more
doaj +1 more source
The genome and antigen proteome analysis of Spiroplasma mirum
Spiroplasma mirum, small motile wall-less bacteria, was originally isolated from a rabbit tick and had the ability to infect newborn mice and caused cataracts. In this study, the whole genome and antigen proteins of S. mirum were comparative analyzed and
Peng Liu +12 more
doaj +1 more source

