Peroxisomal matrix protein import. Suppression of protein import defects in Hansenula polymorpha pex mutants by overproduction of the PTS1 receptor Pex5p.
In the past decade, much progress has been made in understanding the mechanisms that govern sorting of proteins to the peroxisomal lumen. This article summarizes the principal features of how peroxisomal matrix enzymes are thought to reach the peroxisome. In addition, it describes recent data that indicate that, in specific pex mutants of the methylotrophic yeast Hansenula polymorpha, defects in matrix protein import can be (partly) rescued by overproduction of the receptor essential for import of these proteins. The implication of these results on the mechanisms of matrix protein import is discussed.
Kiel
J A
JA
Eukaryotic Microbiology, GBB, University of Groningen, Kerklaan 30, NL-9751 NN Haren, The Netherlands. KielJAKW@Biol.RUG.nl
Veenhuis
M
M
D001692:Biological Transport; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D000074435:Peroxisome-Targeting Signal 1 Receptor; D020675:Peroxisomes / Q000378:metabolism*; D010843:Pichia / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D018160:Receptors, Cytoplasmic and Nuclear / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction
D005656:Fungal Proteins; D000074435:Peroxisome-Targeting Signal 1 Receptor; D018160:Receptors, Cytoplasmic and Nuclear