The N-terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal.
Here we describe the identification of the targeting sequence of peroxisomal amine oxidase (AMO) of H. polymorpha. Deletion analysis revealed that essential targeting information is located within the extreme N-terminal 16 amino acids. Moreover, this sequence can direct a reporter protein to the peroxisomal matrix of H. polymorpha. The N-terminal 16 amino acids of AMO contain a sequence with strong homology to the conserved PTS2 sequence. Therefore, AMO is considered to be a PTS2 protein.
Faber
K N
KN
Department of Microbiology, University of Groningen, Haren, The Netherlands.
Keizer-Gunnink
I
I
Pluim
D
D
Harder
W
W
Ab
G
G
Veenhuis
M
M
D006631:Amine Oxidase (Copper-Containing); D000595:Amino Acid Sequence; D001692:Biological Transport; D008830:Microbodies / Q000378:metabolism*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry* / Q000378:metabolism; D010843:Pichia / Q000201:enzymology*; D021382:Protein Sorting Signals / Q000032:analysis*; D017384:Sequence Deletion
D021382:Protein Sorting Signals; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors