Abstract
We show that the synthesis of the N-terminal 50 amino acids of Pex3p (Pex3p(1-50)) in Hansenula polymorpha pex3 cells is associated with the formation of vesicular membrane structures. Biochemical and ultrastructural findings suggest that the nuclear membrane is the donor membrane compartment of these vesicles. These structures also contain Pex14p and can develop into functional peroxisomes after subsequent reintroduction of the full-length Pex3p protein. We discuss the significance of this finding in relation to peroxisome reintroduction, e.g. in case peroxisomes are lost due to failure in inheritance.
Highlights
Peroxisomes are remarkable among the various classes of cell organelles in that their function and abundance varies dependent on the organism, the environmental conditions, and the physiological state of the cell
We show that the synthesis of the N-terminal 50 amino acids of Pex3p (Pex3p1–50) in Hansenula polymorpha pex3 cells is associated with the formation of vesicular membrane structures
Synthesis of Pex3p1–50 Causes Vesicle Formation in pex3 Cells—Similar to pex3 cells from other organisms, H. polymorpha pex3 cells grown in batch cultures on methanol do not contain detectable peroxisomal membrane remnants, and proteins normally residing in the peroxisomal matrix accumulate in the cytosol
Summary
Peroxisomes are remarkable among the various classes of cell organelles in that their function and abundance varies dependent on the organism, the environmental conditions, and the physiological state of the cell. Peroxisome proliferation can be strictly regulated by growth conditions, ranging from one small organelle when cells are grown in rich media containing glucose, to over 20 during growth of cells on oleate (Saccharomyces cerevisiae, Yarrowia lipolytica, and Pichia pastoris) or methanol (Hansenula polymorpha, P. pastoris) [1, 2]. Under these conditions, peroxisomes house the key enzymes involved in the metabolism of these carbon sources. Present address: Vrije Universiteit Amsterdam, Earth and Life Sciences, Molecular Microbiology, de Boelelaan 1087, 1081 HV Amsterdam, The Netherlands. Mutations in 11 of these human PEX genes have been characterized and shown to be the molecular basis for inherited peroxisome biogenesis disorders, including Zellweger Syndrome, neonatal adrenoleukodystrophy, infantile Refsum’s disease and rhizomelic chondrodysplasia punctata [6, 7]
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