EFFECT OF SITE-DIRECTED MUTAGENESIS OF CONSERVED LYSINE RESIDUES UPON PAS1 PROTEIN FUNCTION IN PEROXISOME BIOGENESIS
EFFECT OF SITE-DIRECTED MUTAGENESIS OF CONSERVED LYSINE RESIDUES UPON PAS1 PROTEIN FUNCTION IN PEROXISOME BIOGENESIS
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DOI：
10.1002/yea.320101210
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发表时间：
1994-12-01
期刊：
影响因子：
2.6
通讯作者：
ERDMANN, R
中科院分区：
文献类型：
--
作者：
KRAUSE, T;KUNAU, WH;ERDMANN, R
Pasl蛋白（Paslp）是酿酒酵母中过氧化物酶体生物合成所需的，并且含有两个推定的ATP结合位点，每个位点在最近表征的AAA家族的成员之间保守的结构域内。为了阐明两个推定的ATP结合位点是否对Paslp功能是必需的，通过定点诱变将第一个推定的ATP结合位点的赖氨酸（467）和第二个推定的ATP结合位点的赖氨酸（744）各自改变为谷氨酸。虽然赖氨酸（744）的替代消除了Pasl蛋白在过氧化物酶体生物合成中的功能，但赖氨酸（467）的替代没有明显的影响。
The Pasl protein (Paslp) 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 Paslp 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 Pasl protein in peroxisome biogenesis, replacement of lysine(467) had no obvious effect.