Author
Minyong Chen
Bio: Minyong Chen is an academic researcher from Ohio State University. The author has contributed to research in topics: Membrane protein & Medicine. The author has an hindex of 11, co-authored 13 publications receiving 1328 citations.
Papers
More filters
TL;DR: It is shown that membrane insertion of two Sec-independent proteins requires YidC, which is essential for E. coli viability and homologues are present in mitochondria and chloroplasts.
Abstract: The basic machinery for the translocation of proteins into or across membranes is remarkably conserved from Escherichia coli to humans. In eukaryotes, proteins are inserted into the endoplasmic reticulum using the signal recognition particle (SRP) and the SRP receptor, as well as the integral membrane Sec61 trimeric complex (composed of alpha, beta and gamma subunits). In bacteria, most proteins are inserted by a related pathway that includes the SRP homologue Ffh, the SRP receptor FtsY, and the SecYEG trimeric complex, where Y and E are related to the Sec61 alpha and gamma subunits, respectively. Proteins in bacteria that exhibit no dependence on the Sec translocase were previously thought to insert into the membrane directly without the aid of a protein machinery. Here we show that membrane insertion of two Sec-independent proteins requires YidC. YidC is essential for E. coli viability and homologues are present in mitochondria and chloroplasts. Depletion of YidC also interferes with insertion of Sec-dependent membrane proteins, but it has only a minor effect on the export of secretory proteins. These results provide evidence for an additional component of the translocation machinery that is specialized for the integration of membrane proteins.
552 citations
TL;DR: YidC is involved in the translocation but not in the targeting of the Procoat protein, because the protein was partitioned into the membrane in the absence of YidC, and studies are consistent with the understanding that YdC cooperates with the Sec translocase for membrane translocation and that YIDC is required for clearing the protein-conducting channel.
148 citations
TL;DR: It is reported that the Sec-independent Pf3 coat protein requires the YidC protein specifically for the membrane translocation step, and the role of YIDC is at the stage of folding the Pf3 protein into a transmembrane configuration.
145 citations
TL;DR: The current status of the protein targeting and membrane integration pathways in E. coli is described and YidC, a recently discovered membrane protein, mediates the membrane integration and folding of hydrophobic domains of membrane proteins.
127 citations
TL;DR: It is shown here that the Sec translocase and the signal recognition particle (SRP) pathway are required for membrane insertion of subunits a and b, and subunit c is integrated into the membrane by the novel YidC pathway.
112 citations
Cited by
More filters
TL;DR: The increasing resistance of microorganisms to conventional chemicals and drugs is a serious and evident worldwide problem that has prompted research into the identification of new biocides with broad activity.
Abstract: The increasing resistance of microorganisms to conventional chemicals and drugs is a serious and evident worldwide problem that has prompted research into the identification of new biocides with broad activity. Plants and their derivatives, such as essential oils, are often used in folk medicine. In nature, essential oils play an important role in the protection of plants. Essential oils contain a wide variety of secondary metabolites that are capable of inhibiting or slowing the growth of bacteria, yeasts and moulds. Essential oils and their components have activity against a variety of targets, particularly the membrane and cytoplasm, and in some cases, they completely change the morphology of the cells. This brief review describes the activity of essential oils against pathogenic bacteria.
1,281 citations
TL;DR: This review summarizes the present knowledge of the mechanism and structure of the Sec translocase, with a special emphasis on unresolved questions and topics of current research.
Abstract: About 25% to 30% of the bacterial proteins function in the cell envelope or outside of the cell. These proteins are synthesized in the cytosol, and the vast majority is recognized as a ribosome-bound nascent chain by the signal recognition particle (SRP) or by the secretion-dedicated chaperone SecB. Subsequently, they are targeted to the Sec translocase in the cytoplasmic membrane, a multimeric membrane protein complex composed of a highly conserved protein-conducting channel, SecYEG, and a peripherally bound ribosome or ATP-dependent motor protein SecA. The Sec translocase mediates the translocation of proteins across the membrane and the insertion of membrane proteins into the cytoplasmic membrane. Translocation requires the energy sources of ATP and the proton motive force (PMF) while the membrane protein insertion is coupled to polypeptide chain elongation at the ribosome. This review summarizes the present knowledge of the mechanism and structure of the Sec translocase, with a special emphasis on unresolved questions and topics of current research.
642 citations
TL;DR: An intuitive introduction to the process of disease transmission is provided, how this stochastic process can be represented mathematically and how this mathematical representation can be used to analyse the emergent dynamics of observed epidemics.
Abstract: The dynamics of infectious diseases are complex, so developing models that can capture key features of the spread of infection is important. Grassly and Fraser provide an introduction to the mathematical analysis and modelling of disease transmission, which, in addition to informing public health disease control measures, is also important for understanding pathogen evolution and ecology.
634 citations
TL;DR: Proteomics has yielded a variety of novel leads for the analysis of protein traffic in B. subtilis and other gram-positive bacteria, which will serve to increase the understanding of virulence factor biogenesis in gram- positive pathogens, which is likely to be of high medical relevance.
Abstract: Secretory proteins perform a variety of important "remote-control" functions for bacterial survival in the environment. The availability of complete genome sequences has allowed us to make predictions about the composition of bacterial machinery for protein secretion as well as the extracellular complement of bacterial proteomes. Recently, the power of proteomics was successfully employed to evaluate genome-based models of these so-called secretomes. Progress in this field is well illustrated by the proteomic analysis of protein secretion by the gram-positive bacterium Bacillus subtilis, for which approximately 90 extracellular proteins were identified. Analysis of these proteins disclosed various "secrets of the secretome," such as the residence of cytoplasmic and predicted cell envelope proteins in the extracellular proteome. This showed that genome-based predictions reflect only approximately 50% of the actual composition of the extracellular proteome of B. subtilis. Importantly, proteomics allowed the first verification of the impact of individual secretion machinery components on the total flow of proteins from the cytoplasm to the extracellular environment. In conclusion, proteomics has yielded a variety of novel leads for the analysis of protein traffic in B. subtilis and other gram-positive bacteria. Ultimately, such leads will serve to increase our understanding of virulence factor biogenesis in gram-positive pathogens, which is likely to be of high medical relevance.
556 citations
TL;DR: It has become clear that hydrophilic as well as hydrophobic preproteins use a common translocase in the outer mitochondrial membrane, but diverge to two distinct translocases in the inner membrane.
Abstract: The vast majority of mitochondrial proteins are synthesized in the cytosol and are imported into mitochondria by protein machineries located in the mitochondrial membranes. It has become clear that hydrophilic as well as hydrophobic preproteins use a common translocase in the outer mitochondrial membrane, but diverge to two distinct translocases in the inner membrane. The translocases are dynamic, high-molecular-weight complexes that have to provide specific means for the recognition of preproteins, channel formation and generation of import-driving forces.
528 citations