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Peroxisomal amine oxidase of Hansenula polymorpha does not require its SRL‐containing C‐terminal sequence for targeting
Author(s) -
Faber Klaas Nico,
Haima Peter,
De Hoop Meltsje Janke,
Harder Wim,
Veenhuis Marten,
Ab Geert
Publication year - 1993
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320090403
Subject(s) - peroxisome , biology , mutant , gene , peroxisomal targeting signal , biochemistry , peptide sequence , microbiology and biotechnology
Amine oxidase (AMO) is a peroxisomal matrix protein of Hansenula polymorpha , which is induced during growth of the yeast in media containing primary amines as a sole nitrogen source. The deduced amino acid sequence of the protein contains an SRL sequence at nine amino acids from the C‐terminus. In this study, we have examined the possible role of the SRL motif in sorting of AMO to peroxisomes by mutating the corresponding gene sequence. For this purpose, we have developed a DNA construct that is specifically integrated into the AMO locus of the H. polymorpha genome, placing the mutant gene under the control of the endogenous AMO promoter and eliminating expression of the wild‐type gene. Analysis of a stable transformant, containing the desired gene configuration, showed that mutation of the C‐terminal sequence neither interfered with correct targeting of the protein into the peroxisome nor displayed significant effects on its activity. From this, it was concluded that the SRL‐containing C‐terminus is not essential for peroxisomal targeting of AMO in H. polymorpha .