Results 11 to 20 of about 3,879 (192)

The protein-conducting channel SecYEG [PDF]

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2004
In bacteria, the translocase mediates the translocation of proteins into or across the cytosolic membrane. It consists of a membrane embedded protein-conducting channel and a peripherally associated motor domain, the ATPase SecA. The channel is formed by
Driessen, AM   +3 more
core   +13 more sources

The Dynamic SecYEG Translocon [PDF]

open access: yesFrontiers in Molecular Biosciences, 2021
The spatial and temporal coordination of protein transport is an essential cornerstone of the bacterial adaptation to different environmental conditions.
Julia Oswald   +7 more
doaj   +4 more sources

YidC and SecYEG form a heterotetrameric protein translocation channel [PDF]

open access: yesScientific Reports, 2017
The heterotrimeric SecYEG complex cooperates with YidC to facilitate membrane protein insertion by an unknown mechanism. Here we show that YidC contacts the interior of the SecY channel resulting in a ligand-activated and voltage-dependent complex with ...
Ilie Sachelaru   +9 more
doaj   +4 more sources

The TerC family metal chaperone MeeY enables surfactin export in Bacillus subtilis [PDF]

open access: yesJournal of Bacteriology
TerC family proteins are widely conserved integral membrane proteins with functions related to metal transport. In Bacillus subtilis, the TerC proteins MeeF and MeeY play overlapping roles in the metalation of manganese-requiring membrane and ...
Bixi He   +4 more
doaj   +2 more sources

MultiPassMerger: Automated data processing for multipass cyclic ion mobility HDX-MS. [PDF]

open access: yesProtein Sci
Abstract Hydrogen/deuterium exchange‐mass spectrometry (HDX‐MS) is a powerful tool for studying protein structure and dynamics. As a bottom‐up LC‐MS technique, its success largely depends on peptide identifications made by peptide mapping prior to HDX measurements.
Duerr V, Griffiths D, Politis A.
europepmc   +2 more sources

SecYEG-mediated translocation in a model synthetic cell. [PDF]

open access: yesSynth Biol (Oxf)
Abstract Giant unilamellar vesicles (GUVs) provide a powerful model compartment for synthetic cells. However, a key challenge is the incorporation of membrane proteins that allow for transport, energy transduction, compartment growth and division.
Schoenmakers LLJ   +5 more
europepmc   +6 more sources

The Multifunctional Preprotein Binding Domain of SecA. [PDF]

open access: yesChembiochem
SecA protein has evolved to perform multiple tasks. Its Preprotein Binding Domain (PBD) is a key module, adopting three conformational states. The PBD's inter‐ and intra‐protomeric interactions, along with biophysical data, reveal the influence of these states on the translocation process.
Giotas E   +2 more
europepmc   +2 more sources

High Efficacy of Rose Bengal in Reducing the Pathogenicity of <i>Escherichia coli</i> Isolated From Diarrheal Infections. [PDF]

open access: yesInt J Microbiol
Diarrheal infections, a leading cause of global morbidity and mortality, are frequently attributed to pathogenic Escherichia coli strains. The rise of antibiotic resistance among these pathogens necessitates the exploration of alternative therapeutic agents.
Malanda CDB   +7 more
europepmc   +2 more sources

Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane of E. coli

open access: yesFrontiers in Molecular Biosciences, 2022
Protein integration into biomembranes is an essential biological phenomenon common to all organisms. While various factors involved in protein integration, such as SRP, SecYEG and YidC, are proteinaceous, we identified a glycolipid named MPIase (Membrane
Hanako Nishikawa   +6 more
doaj   +1 more source

Opening the SecYEG Protein Translocon [PDF]

open access: yesBiophysical Journal, 2009
The Sec61/SecYEG translocon is the central component of the major biosynthetic pathway for membrane and secreted proteins. To incorporate membrane proteins into the endoplasmic reticulum membrane of eukaryotes (Sec61), or into the plasma membrane of prokaryotes (SecYEG), the translocon relies on the opening of a lateral helical gate formed by ...
Bondar, Ana Nicoleta   +2 more
openaire   +2 more sources

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