Conformational Dynamics of the Plug Domain of the SecYEG Protein-conducting Channel [PDF]
The central pore of the SecYEG preprotein-conducting channel is closed at the periplasmic face of the membrane by a plug domain. To study its conformational dynamics, the plug was labeled site-specifically with an environment-sensitive fluorophore.
Arkowitz +44 more
core +2 more sources
In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis. [PDF]
The majority of proteins that are secreted across the bacterial cytoplasmic membrane leave the cell via the Sec pathway, which in its minimal form consists of the dimeric ATP-driven motor protein SecA that associates with the protein-conducting membrane ...
Irfan Prabudiansyah +2 more
doaj +1 more source
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 +2 more sources
In this mini review, we bring into the spotlight bacterial extracellular membrane vesicle engineering to encase bacterial immunomodulatory effectors into their cargo for their application as biocontrol agents. The overarching goal is achieving plant priming by deploying its innate immune responses thereby preventing upcoming infections.
Irene Jiménez‐Guerrero +3 more
wiley +1 more source
The Lateral Gate of SecYEG Opens during Protein Translocation [PDF]
The SecYEG translocon of Escherichia coli mediates the translocation of preproteins across the cytoplasmic membrane. Here, we have examined the role of the proposed lateral gate of the translocon in translocation. A dual cysteine cross-linking approach allowed the introduction of cross-linker arms of various lengths between adjoining aminoacyl ...
du Plessis, D.J.F. +3 more
openaire +3 more sources
Probing macromolecular crowding at the lipid membrane interface with genetically‐encoded sensors
Abstract Biochemical processes within the living cell occur in a highly crowded environment, where macromolecules, first of all proteins and nucleic acids, occupy up to 30% of the volume. The phenomenon of macromolecular crowding is not an exclusive feature of the cytoplasm and can be observed in the densely protein‐packed, nonhomogeneous cellular ...
Maryna Löwe +5 more
wiley +1 more source
Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC [PDF]
Protein secretion and membrane insertion occur through the ubiquitous Sec machinery. In this system, insertion involves the targeting of translating ribosomes via the signal recognition particle and its cognate receptor to the SecY (bacteria and archaea)/
Alvira-de-Celis, Sara +10 more
core +4 more sources
Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control. [PDF]
Green fluorescent protein (GFP) has undergone a long history of optimization to become one of the most popular proteins in all of cell biology. It is thermally and chemically robust and produces a pronounced fluorescent phenotype when expressed in cells ...
Adam C Fisher, Matthew P DeLisa
doaj +1 more source
Evaluating the oligomeric state of SecYEG in preprotein translocase [PDF]
SecA insertion and deinsertion through SecYEG drive preprotein translocation at the Escherichia coli inner membrane. We present three assessments of the theory that oligomers of SecYEG might form functional translocation sites. (i) Formaldehyde cross- linking of translocase reveals cross-links between SecY, SecE and SecG, but not higher order oligomers.
T L, Yahr, W T, Wickner
openaire +2 more sources
Yet another job for the bacterial ribosome
The ribosome is a sophisticated cellular machine, composed of RNA and protein, which translates the mRNA-encoded genetic information into protein and thus acts at the center of gene expression. Still, the ribosome not only decodes the genetic information,
Andrea Origi +6 more
doaj +1 more source

