Normal peroxisome development from vesicles induced by truncated Hansenula polymorpha Pex3p.
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.
Faber
Klaas Nico
KN
Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Postbus 14, 9750 AA Haren, The Netherlands. k.n.faber@med.rug.nl
Haan
Gert Jan
GJ
Baerends
Richard J S
RJ
Kram
Anita M
AM
Veenhuis
Marten
M
D018528:ATP-Binding Cassette Transporters; D001483:Base Sequence; D017931:DNA Primers; D005656:Fungal Proteins / Q000502:physiology*; D008565:Membrane Proteins / Q000502:physiology*; D008856:Microscopy, Fluorescence; D009685:Nuclear Envelope / Q000378:metabolism; D000074401:Peroxins; D020675:Peroxisomes / Q000378:metabolism*; D010843:Pichia / Q000378:metabolism* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins
D018528:ATP-Binding Cassette Transporters; D017931:DNA Primers; D005656:Fungal Proteins; D008565:Membrane Proteins; C070895:PEX3 protein, S cerevisiae; D000074401:Peroxins; C406793:SPF1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins