C-terminus of p47(phox) is required for interaction with leukocyte type rat 12-lipoxygenase.
In yeast two-hybrid system, rat 12-lipoxygenase (12-LO) bound to complete (390 amino acids) or the N-terminus truncated form of human p47 (phox), but not to the C-terminus truncated form (residues 1-286). When glutathione S-transferase fused human p47(phox) was added to an in vitro 12-LO enzyme activity assay, formation of 12-hydroperoxyeicosatetraenoic acid was reduced significantly compared to the C-terminus truncated form. These results indicate that C-terminus of p47(phox) is important for its interaction to rat 12-LO.
Tanabe
Michiharu
M
Department of Medical Biochemistry and Biophysics, Karolinska Instituet, Stockholm, Sweden.
Kamitani
Hideki
H
Watanabe
Takashi
T
Rådmark
Olof
O
D000818:Animals; D001092:Arachidonate 12-Lipoxygenase / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007962:Leukocytes / Q000201:enzymology*; D019255:NADPH Oxidases; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020798:Two-Hybrid System Techniques
D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; D001092:Arachidonate 12-Lipoxygenase; D019255:NADPH Oxidases; C060505:neutrophil cytosolic factor 1