Effect of site-directed mutagenesis of conserved lysine residues upon Pas1 protein function in peroxisome biogenesis.
The Pas1 protein (Pas1p) is required for peroxisome biogenesis in Saccharomyces cerevisiae and contains two putative ATP-binding sites, each within a domain which is conserved among members of the recently characterized AAA-family. To elucidate whether both putative ATP-binding sites are essential for Pas1p function, lysine 467 of the first and lysine 744 of the second putative ATP-binding site were each changed to glutamate by site-directed mutagenesis. While replacement of lysine 744 abolished the function of the Pas1 protein in peroxisome biogenesis, replacement of lysine 467 had no obvious effect.
Krause
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Abteilung für Zellbiochemie, Medizinische Fakultät, Ruhr-Universität Bochum, Germany.
Kunau
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Erdmann
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D000074183:ATPases Associated with Diverse Cellular Activities; D000251:Adenosine Triphosphatases; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D005656:Fungal Proteins / Q000502:physiology*; D008239:Lysine; D008565:Membrane Proteins / Q000502:physiology*; D008830:Microbodies / Q000502:physiology*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D029701:Saccharomyces cerevisiae Proteins; D013329:Structure-Activity Relationship
D005656:Fungal Proteins; D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D000074183:ATPases Associated with Diverse Cellular Activities; C511586:PEX1 protein, S cerevisiae; D008239:Lysine