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The N‐terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal
Author(s) -
Faber Klaas Nico,
Keizer-Gunnink Ineke,
Pluim Dick,
Harder Wim,
Geert AB,
Veenhuis Marten
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01317-t
Subject(s) - peroxisome , peroxisomal targeting signal , chemistry , biochemistry , amine oxidase , amine gas treating , signal peptide , microbiology and biotechnology , biology , enzyme , peptide sequence , receptor , gene , organic chemistry
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.