Watermelon glyoxysomal malate dehydrogenase is sorted to peroxisomes of the methylotrophic yeast, Hansenula polymorpha

FEBS Letters

Keizer-Gunnink, I.¹  van der Klei, I.J.¹  Veenhuis, M.¹  Faber, K.N.¹  Harder, W.¹  Gietl, C.² 

[1] Laboratory for Electron Microscopy, Biological Centre, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands;Institute for Botany and Microbiology, Technical University of Munich, Arcisstraße 16, D-80333 Munich, Germany

关键词: Malate dehydrogenase;    Glyoxysome;    Peroxisome;    Hansenula polymorpha;    Citrullus vulgaris;    Protein targeting;   

DOI  :  10.1016/0014-5793(93)81697-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have studied the fate of the watermelon (Citrullus vulgaris Schrad.) glyoxysomal enzyme, malate dehydrogenase (gMDH), after synthesis in the methylotrophic yeast, Hansenula polymorpha. The gene encoding the precursor form of gMDH (pre-gMDH) was cloned in an H. polymorpha expression vector downstream of the inducible H. polymorpha alcohol oxidase promoter. During methylotrophic growth, pre-gMDH was synthesized and imported into peroxisomes, where it was enzymatically active. The apparent molecular mass of the protein located in H. polymorpha peroxisomes was equal to that of pre-gMDH (41 kDa), indicating that N-terminal processing of the transit peptide had not occurred in the yeast.

【 授权许可】

Unknown