Ohsumi, Y. Unified nomenclature for yeast autophagy-related genes. Cell 5: Hazra, P. Peroxisome remnants in pex3D cells and the requirement of Pex3p for interactions between the peroxisomal docking and translocation subcomplexes. Traffic, 3: Import of proteins into peroxisomes. In Protein targeting, transport and translocation , eds.
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Dalbey, R. Hitchhiking fads en route to peroxisomes. Luers, G.
Genomic organization, chromosomal localization and tissue specific expression of the murine Pxmp2 gene encoding the 22 kDa peroxisomal membrane protein Pmp Gene, Self destruction in the line of duty. Cell, 1: Dammai, V. The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisome matrix and recycled to the cytosol.
Amery, L. Combinatorial Chem. Johnson, M. Yeast, Quantitative analysis of peroxisomal protein import in vitro. Cell Res. Sakai, Y. Environmental response of yeast peroxisomes: aspects of organelle assembly and degradation. Cell Biochemistry and Biophysics, Snyder, W.
The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane.
Koller, A. Import of peroxisomal matrix and membrane proteins. Pex17p is required for import of both peroxisome membrane and lumenal proteins and interacts with Pex19p and the PTS-receptor docking complex in Pichia pastoris. Yamashita, H. Characterization of the human and murine PMP20 peroxisomal membrane proteins that exhibit antioxidant activity in vitro. Pex22p of Pichia pastoris, essential for peroxisomal matrix protein import, anchors the ubiquitin-conjugating enzyme, Pex4p, on the peroxisomal membrane.
EMBO J. Analysis of the peroxisomal Acyl-CoA oxidase gene product from Pichia pastoris and determination of its targeting signal. Pex19p interacts with Pex3p and Pex10p and is essential for peroxisome biogenesis in Pichia pastoris. Fransen, M. H , pp, Springer-Verlag USA, Kostrub, C. Hus1p, a conserved fission yeast checkpoint protein, interacts with Rad1p and is phosphorylated in response to DNA damage. Peroxisome degradation by microautophagy in Pichia pastoris: identification of specific steps and morphological intermediates.
The P. Elgersma, Y. A mobile PTS2-receptor for peroxisomal protein import in Pichia pastoris. Faber, K.
Dissection of Aberrant GPCR Signaling in Tumorigenesis – A Systems Biology Approach
Components involved in peroxisome import, biogenesis, proliferation, turnover and movement. Osman, F. Double-strand break-induced recombination in eukaryotes. Acids Res. Use of Pichia pastoris as a model eukaryotic system: Peroxisome biogenesis, in Methods in Molecular Biology: Pichia protocols ed. PEX genes on the rise. Nature Genetics, Wiemer, E. Distel, B. A unified nomenclature for peroxisome biogenesis. Terlecky, S. Protein translocation into peroxisomes. Isolation and characterization of Pas2p, a peroxisomal membrane protein essential for peroxisome biogenesis in the methylotrophic yeast Pichia pastoris.
Knudsen, K. USA Converging models of peroxisome biogenesis. Fortunato, E. When the lock reforms, we see the structure return to its inactive conformation. We also find that the ionic lock exists in three states: closed or locked , semi-open with a bridging water mol. The interconversion of these states involves the concerted motion of the entire protein. We characterize these states and the concerted motion underlying their interconversion.
These findings may help elucidate the connection between key local events and the assocd.
Activation of G protein-coupled receptors GPCRs is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle contg. In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption. Such a trigger by the chromophore corresponds to binding of a diffusible ligand to other GPCRs.
Here we have explored the functional role of water mols. The structural model suggests that water mols. To confirm the physiol. A new high-resoln. Substantial improvement of the resoln.
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The new structure completely resolves the polypeptide chain and provides further details of the chromophore binding site including the configuration about the C6-C7 single bond of the cis-retinal Schiff base. Based on both an earlier structure and the new improved model of the protein, a theor. The consistency between the exptl. Importantly, the new crystal structure refinement reveals significant neg. Bond alternation along the unsatd. Other differences between the exptl.
Li, Jade; Edwards, Patricia C. We have detd. The new structure reveals mechanistically important details unresolved previously, which are considered in the membrane context by docking the structure into a cryo-electron microscopy map of 2D crystals. Kinks in the transmembrane helixes facilitate inter-helical polar interactions. Ordered water mols.
Glu forms a complex with a water mol.