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A unifying mechanism for protein transport through the core bacterial Sec machinery

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Summary: Secretory proteins are translocated across lipid membranes via protein-conducting channels called SecY in prokaryotes and Sec61 in eukaryotes. SecA, an ATPase, drives the posttranslational translocation of secretory proteins in bacteria through the SecY channel. The mechanism of how SecA moves a polypeptide chain through the SecY channel is poorly understood. This study presents electron cryomicroscopy structures of the active SecA-SecY translocon with a polypeptide substrate, revealing the conformational changes of SecA and the structural basis of polypeptide movement during translocation.

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Summary: Gram-negative bacteria have a protein-rich envelope crucial for various functions like energy production and protection against environmental challenges. Proteins are transported through the envelope by molecular chaperones like SurA. The interaction between SurA and the Sec-machinery helps prevent protein aggregation and degradation, ensuring safe passage of proteins to the periplasm and outer-membrane.

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Summary: The Omp85 protein superfamily is a group of proteins found in the outer membrane of gram-negative bacteria and bacterial-origin eukaryotic organelles. These proteins are involved in both membrane insertion and translocation of proteins across the outer membrane. Recent studies have uncovered new insights into the functions of these proteins, particularly the well-studied member BamA, which is essential for bacterial barrel assembly and has potential implications for antibiotic development.

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Unsaturated fatty acids augment protein transport via the SecA:SecYEG translocon

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Summary: Unsaturated fatty acids (UFAs) play a crucial role in enhancing protein translocation mediated by SecA: SecYEG in bacterial cytoplasmic membranes. UFAs increase lipid area and cause loose packing of lipid head groups, promoting SecA binding and improving translocation efficiency. This discovery highlights the importance of fatty acid structure in protein secretion mechanisms in bacteria, which respond to environmental changes by altering their membrane composition.

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Summary: By measuring the fluorescence intensity and wavelength shift change of the polarity-sensitive fluorophore NBD, we determined the disposition of SecA on the Escherichia coli membrane. Our results showed that SecA is primarily anchored in the membrane interface by the positive charges of the N terminus domain, and a region of the nucleotide binding domain II is also important for binding. The topology of SecA on the membrane is consistent with previous structural observations.

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Summary: Transport of proteins across and into membranes is a fundamental process in biology. Recent studies have shown that the diffusion of arginine residues limits pre-protein transport, while lysine can be transported across membranes in its neutral form. These findings have implications for understanding the mechanism of protein secretion and suggest a potential role of proton-motive force in aiding transport.
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Summary: This article provides an overview of systems and processes involved in the membrane translocation of folded proteins. It discusses various mechanisms for protein translocation, including pore/channel formation, local membrane disruption, membrane thinning, and transport by membrane vesicles. The article also introduces a newly discovered vesicular transport mechanism, vesicle budding and collapse, as a potential unifying mechanism for folded protein translocation processes.

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