THE N-TERMINUS OF AMINE OXIDASE OF HANSENULA-POLYMORPHA CONTAINS A PEROXISOMAL TARGETING SIGNAL

Here we describe the identification of the targeting sequence of perox isomal amine oxidase (AMO) of H. polymorpha. Deletion analysis reveale d that essential targeting information is located within the extreme N -terminal 16 amino acids. Moreover, this sequence can direct a reporte r protein to the peroxisomal matrix of H. polymorpha. The N-terminal 1 6 amino acids of AMO contain a sequence with strong homology to the co nserved PTS2 sequence. Therefore, AMO is considered to be a PTS2 prote in.