The N‐terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal

FEBS Letters

Harder, Wim¹  Keizer-Gunnink, Ineke¹  Faber, Klaas Nico¹  Geert, AB²  Pluim, Dick¹  Veenhuis, Marten¹ 

[1] Department of Microbiology, Biological Centre, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands;Laboratory of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

关键词: Peroxisome;    Topogenic signal;    Amine oxidase;    PTS2;    β-Lactamase;    Watermelon malate dehydrogenase;   

DOI  :  10.1016/0014-5793(94)01317-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown