Normal peroxisome development from vesicles induced by truncated Hansenula polymorpha Pex3pFaber, KN., Haan, GJ., Baerends, RJS., Kram, AM. & Veenhuis, M., 29-Mar-2002, In : The Journal of Biological Chemistry. 277, 13, p. 11026-11033 8 p.
Research output: Contribution to journal › Article › Academic › peer-review
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.
|Number of pages||8|
|Journal||The Journal of Biological Chemistry|
|Publication status||Published - 29-Mar-2002|
- DIHYDROXYACETONE SYNTHASE, SELECTIVE INACTIVATION, ENDOPLASMIC-RETICULUM, DEFICIENT MUTANTS, TARGETING SIGNAL, PICHIA-PASTORIS, ALCOHOL OXIDASE, N-TERMINUS, BIOGENESIS, MEMBRANE