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Watermelon glyoxysomal malate dehydrogenase is sorted to peroxisomes of the methylotrophic yeast, Hansenula polymorpha
Author(s) -
van der Klei I.J.,
Faber K.N.,
Keizer-Gunnink I.,
Gietl C.,
Harder W.,
Veenhuis M.
Publication year - 1993
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(93)81697-x
Subject(s) - peroxisome , biochemistry , yeast , biology , malate dehydrogenase , dehydrogenase , enzyme , gene
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.