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 SecYEG, a multimeric protein complex that assembles into oligomeric forms. The structure and subunit composition of this protein-conducting channel is evolutionary conserved and a similar system is found in the endoplasmic reticulum of eukaryotes and the cytoplasmic membrane of archaea. The ribosome and other membrane proteins can associate with the protein-conducting channel complex and affect its activity or functionality.
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Analysis and prediction of internal mitochondrial targeting signals.
Methods Enzymol
October 2024
Computational Systems Biology, RPTU University of Kaiserslautern-Landau, Kaiserslautern, Germany. Electronic address:
Mitochondria consist of several hundreds of proteins, the vast majority of which are synthesized in the cytosol as precursor proteins from where they are targeted to and imported into mitochondria. The transport of proteins into mitochondria relies on specific targeting information encoded within the protein sequence, known as mitochondrial targeting sequences (MTSs). These N-terminal extensions are usually between 8 and 80 residues long and form amphipathic helices with one hydrophobic and one positively charged surface.
View Article and Find Full Text PDFRole of Sec61α2 Translocon in Insulin Biosynthesis.
Diabetes
December 2024
Division of Metabolism, Endocrinology & Diabetes, University of Michigan Medical School, Ann Arbor, MI.
Translocational regulation of proinsulin biosynthesis in pancreatic β-cells is unknown, although several studies have reported an important accessory role for the Translocon-Associated Protein complex to assist preproinsulin delivery into the endoplasmic reticulum via the heterotrimeric Sec61 translocon (comprising α, β, and γ subunits). The actual protein-conducting channel is the α-subunit encoded either by Sec61A1 or its paralog Sec61A2. Although the underlying channel selectivity for preproinsulin translocation is unknown, almost all studies of Sec61α to date have focused on Sec61α1.
View Article and Find Full Text PDFTracking the Activity and Position of Mitochondrial β-Barrel Proteins.
Methods Mol Biol
March 2024
Biophysics Department, Institute of Biomaterials and Biomolecular Systems, University of Stuttgart, Stuttgart, Germany.
Total interference reflection fluorescence (TIRF) microscopy of lipid bilayers is an effective technique for studying the lateral movement and ion channel activity of single integral membrane proteins. Here we describe how to integrate the mitochondrial outer membrane preprotein translocase TOM-CC and its β-barrel protein-conducting channel Tom40 into supported lipid bilayers to identify possible relationships between movement and channel activity. We propose that our approach can be readily applied to membrane protein channels where transient tethering to either membrane-proximal or intramembrane structures is accompanied by a change in channel permeation.
View Article and Find Full Text PDFMolecular view of ER membrane remodeling by the Sec61/TRAP translocon.
EMBO Rep
December 2023
Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Protein translocation across the endoplasmic reticulum (ER) membrane is an essential step during protein entry into the secretory pathway. The conserved Sec61 protein-conducting channel facilitates polypeptide translocation and coordinates cotranslational polypeptide-processing events. In cells, the majority of Sec61 is stably associated with a heterotetrameric membrane protein complex, the translocon-associated protein complex (TRAP), yet the mechanism by which TRAP assists in polypeptide translocation remains unknown.
View Article and Find Full Text PDFStructural basis of mitochondrial protein import by the TIM23 complex.
Nature
September 2023
Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA.
Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope. Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits of the TIM23 complex, the essential multipass membrane protein Tim23, together with the evolutionarily related protein Tim17, has long been postulated to form a protein-conducting channel.
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