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Yarrowia lipolytica Pex20p, Saccharomyces cerevisiae Pex18p/Pex21p and mammalian Pex5pL fulfil a common function in the early steps of the peroxisomal PTS2 import pathway
It is shown here that the early steps of protein import into peroxisomes exhibit a greater similarity than was thought previously to be the case.
Recombinant Human Peroxisomal Targeting Signal Receptor PEX5
- W. Schliebs, J. Saidowsky, B. Agianian, G. Dodt, F. Herberg, W. Kunau
- Biology, ChemistryThe Journal of Biological Chemistry
- 26 February 1999
Surface plasmon resonance analysis indicates that PEX5 binds to the N-terminal fragment of PEX14-(1–78) with a very high affinity in the low nanomolar range, and a pentapeptide motif that is reiterated seven times in Pex5 is proposed as a determinant for the interaction with PEX 14.
MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization
MINOS1/Mio10 is a novel constituent of the mitofilin/Fcj1 complex of the inner membrane, linking the morphology phenotype of the mutant to the activity of the mitochondrial inner membrane organizing complex.
The peroxisomal importomer constitutes a large and highly dynamic pore
It is demonstrated that the membrane-associated import receptor Pex5p together with its docking partner Pex14p forms a gated ion-conducting channel which can be opened to a diameter of about 9 nm by the cytosolic receptor–cargo complex.
Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p.
Proteomics Characterization of Mouse Kidney Peroxisomes by Tandem Mass Spectrometry and Protein Correlation Profiling*S
This work uses classical subcellular fractionation in combination with MS-based proteomics methodologies to characterize the proteome of mouse kidney peroxisomes and believes to have compiled the so far most comprehensive protein catalogue of mammalian per oxisomes.
Peroxisomal matrix protein import: the transient pore model
A mechanistic model is proposed that conceptually divides the import process into three consecutive steps: the formation of a translocation pore by the import receptor, the ubiquitylation of the import receptors, and pore disassembly/receptor recycling.
The Di-aromatic Pentapeptide Repeats of the Human Peroxisome Import Receptor PEX5 Are Separate High Affinity Binding Sites for the Peroxisomal Membrane Protein PEX14*
It is demonstrated that the evolutionarily conserved pentapeptide repeat motifs, WX(E/D/Q/A/S)(E/ D/Q)(F/Y), in PEX5 bind to PEX14 with high affinity, and proposed that the side chains of the aromatic amino acids are in close proximity as part of an amphipathic α-helix and together form hydrophobic anchors for binding P EX5 to individual PEX 14 molecules.
Pex14p, more than just a docking protein.
A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.
A monomeric double-mutation variant of TIM, expressed in Escherichia coli, purified to homogeneity, and biochemically characterized shows that RE-TIM is a monomer in solution and implies that wild type monomersic subunits have some stability and are catalytically active.