YidC from Escherichia coli Forms an Ion-Conducting Pore upon Activation by Ribosomes [PDF]
Biomolecules, 2023 The universally conserved protein YidC aids in the insertion and folding of transmembrane polypeptides. Supposedly, a charged arginine faces its hydrophobic lipid core, facilitating polypeptide sliding along YidC’s surface.
Denis G. Knyazev +9 more
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Cardiolipin occupancy profiles of YidC paralogs reveal the significance of respective TM2 helix residues in determining paralog-specific phenotypes [PDF]
Frontiers in Molecular Biosciences, 2023 YidC belongs to an evolutionarily conserved family of insertases, YidC/Oxa1/Alb3, in bacteria, mitochondria, and chloroplasts, respectively. Unlike Gram-negative bacteria, Gram-positives including Streptococcus mutans harbor two paralogs of YidC.
Surabhi Mishra +3 more
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An investigation of the YidC-mediated membrane insertion of Pf3 coat protein using molecular dynamics simulations [PDF]
Frontiers in Molecular Biosciences, 2022 YidC is a membrane protein that facilitates the insertion of newly synthesized proteins into lipid membranes. Through YidC, proteins are inserted into the lipid bilayer via the SecYEG-dependent complex.
Adithya Polasa +3 more
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Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane of E. coli [PDF]
Frontiers 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
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Evolution of mitochondrial TAT translocases illustrates the loss of bacterial protein transport machines in mitochondria [PDF]
BMC Biology, 2018 Background Bacteria and mitochondria contain translocases that function to transport proteins across or insert proteins into their inner and outer membranes. Extant mitochondria retain some bacterial-derived translocases but have lost others.
Markéta Petrů +5 more
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The Role of Protein–Lipid Interactions in Priming the Bacterial Translocon [PDF]
MembranesProtein–lipid interactions demonstrate important regulatory roles in the function of membrane proteins. Nevertheless, due to the semi-liquid nature and heterogeneity of biological membranes, and dissecting the details of such interactions at high ...
Matt Sinclair, Emad Tajkhorshid
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Features of membrane protein sequence direct post-translational insertion [PDF]
Nature CommunicationsThe proper folding of multispanning membrane proteins (MPs) hinges on the accurate insertion of their transmembrane helices (TMs) into the membrane. Predominantly, TMs are inserted during protein translation, via a conserved mechanism centered around the
Ilya A. Kalinin +6 more
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Phosphoproteomics analysis of acid stress response of Alicyclobacillus acidoterrestris in response to acid stress [PDF]
Applied Microbiology and BiotechnologyAlicyclobacillus acidoterrestris causes pasteurized acidic juices spoilage, resulting in a significant decline in juice quality and causing economic losses. Exploration of A.
Yingli Liu +5 more
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Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery [PDF]
Nature CommunicationsRegulatory arrest peptides interact with specific residues on bacterial ribosomes and arrest their own translation. Here, we analyse over 30,000 bacterial genome sequences to identify additional Sec/YidC-related arrest peptides, followed by in vivo and ...
Keigo Fujiwara +4 more
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B. subtilis Sec and Srp Systems Show Dynamic Adaptations to Different Conditions of Protein Secretion [PDF]
CellsSecA is a widely conserved ATPase that drives the secretion of proteins across the cell membrane via the SecYEG translocon, while the SRP system is a key player in the insertion of membrane proteins via SecYEG. How SecA gains access to substrate proteins
Svenja M. Fiedler, Peter L. Graumann
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