-transparent.png){kind=logo}
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.
Related Publications
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
April 1992,
Yeast (Chichester, England),
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
July 1989,
Biochimica et biophysica acta,
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
June 1992,
FEBS letters,
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
April 1993,
Yeast (Chichester, England),
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
November 2003,
European journal of biochemistry,
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
May 2007,
FEBS letters,
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
December 1994,
Proceedings of the National Academy of Sciences of the United States of America,
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
August 2005,
Journal of cell science,
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
January 2006,
FEBS letters,
K N Faber, and
I Keizer-Gunnink, and
D Pluim, and
W Harder, and
G Ab, and
M Veenhuis
October 2007,
FEMS yeast research,
