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Effect of site‐directed mutagenesis of conserved lysine residues upon Pas1 protein function in peroxisome biogenesis
Author(s) -
Krause Thomas,
Kunau WolfH.,
Erdmann Ralf
Publication year - 1994
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.320101210
Subject(s) - biology , lysine , biogenesis , mutagenesis , site directed mutagenesis , peroxisome , saccharomyces cerevisiae , function (biology) , biochemistry , genetics , conserved sequence , amino acid , mutation , gene , peptide sequence , mutant
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.