Clofibrate-inducible, 28-kDa peroxisomal integral membrane protein is encoded by PEX11

• Autor: Abe, Isao ; Okumoto, Kanji ; Tamura, Shigehiko ; Fujiki, Yukio
• Assuntos: Amino Acid Sequence ; Animals ; Antibodies - immunology ; Base Sequence ; CG, complementation group ; CHO Cells ; Clofibrate ; Clofibrate - pharmacology ; Cloning, Molecular ; Complementation group ; Cricetinae ; Dilysine motif ; DNA Primers ; DNA, Complementary ; EST, expressed sequence tag ; Fungal Proteins - genetics ; Fungal Proteins - immunology ; Gene Expression Regulation - drug effects ; Humans ; Male ; Membrane protein ; Membrane Proteins - genetics ; Membrane Proteins - immunology ; Microbodies - metabolism ; Molecular Sequence Data ; Peroxin ; Peroxins ; Peroxisome biogenesis ; PEX11, cDNA encoding the peroxin Pex11p ; PMP28, 28-kDa peroxisomal membrane protein ; PTS1, peroxisome targeting signal type 1 ; Rats ; Rats, Inbred F344 ; Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid
• É parte de: FEBS letters, 1998-07, Vol.431 (3), p.468-472
• Notas: ObjectType-Article-1
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• Descrição: We cloned a human PEX11 cDNA by expressed sequence tag homology search using yeast Candida boidinii PEX11, followed by screening of human liver cDNA library. PEX11 encoded a peroxisomal protein Pex11p comprising 247 amino acids, with two transmembrane segments and a dilysine motif at the C-terminus. Pex11p comigrated in SDS-PAGE with a 28-kDa peroxisomal integral membrane protein (PMP28) isolated from the liver of clofibrate-treated rats and was crossreactive to anti-PMP28 antibody, thereby indicating PEX11 to encode PMP28. Pex11p exposes both N- and C-terminal parts to the cytosol. PEX11 was not responsible for ten complementation groups of human peroxisome deficiency disorders.
  
• Editor: England: Elsevier B.V
  
• Idioma: Inglês