Targeting signal of the peroxisomal catalase in the methylotrophic yeast Hansenula polymorpha.
The methylotrophic yeast, Hansenula polymorpha, harbours a unique catalase (EC 1.11.1.6), which is essential for growth on methanol as a carbon source and is located in peroxisomes. Its corresponding gene has been cloned and the nucleotide sequence determined. The deduced amino acid sequence displayed the tripeptide serine-lysine-isoleucine at the extreme C-terminus, which is similar to sequences of other peroxisomal targeting signals. Exchange of the ultimate amino acid, isoleucine, of catalase for serine revealed a cytosolic enzyme activity and a concomitant loss of peroxisome function. We concluded that the tripeptide is essential for targeting of catalase in H. polymorpha.
Didion
T
T
Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Germany.
Roggenkamp
R
R
D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D002374:Catalase / Q000235:genetics* / Q000378:metabolism; D002499:Centrifugation, Density Gradient; D004271:DNA, Fungal; D007700:Kinetics; D008830:Microbodies / Q000201:enzymology*; D008969:Molecular Sequence Data; D010843:Pichia / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D021382:Protein Sorting Signals / Q000235:genetics* / Q000378:metabolism
D004271:DNA, Fungal; D021382:Protein Sorting Signals; D002374:Catalase