title: The N-terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal.
abstract: 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.
authors: Department of Microbiology, University of Groningen, Haren, The Netherlands.
authors: K N
authors: KN
authors: Faber
authors: I
authors: I
authors: Keizer-Gunnink
authors: D
authors: D
authors: Pluim
authors: W
authors: W
authors: Harder
authors: G
authors: G
authors: Ab
authors: M
authors: M
authors: Veenhuis
mesh_terms: 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
chemical_list: D021382:Protein Sorting Signals; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors