EFFECT OF SITE-DIRECTED MUTAGENESIS OF CONSERVED LYSINE RESIDUES UPON PAS1 PROTEIN FUNCTION IN PEROXISOME BIOGENESIS

被引：15

作者：

KRAUSE, T ^{[1
]}

KUNAU, WH ^{[1
]}

ERDMANN, R ^{[1
]}

机构：

[1] RUHR UNIV BOCHUM,FAK MED,INST PHYSIOL CHEM,ZELLBIOCHEM ABT,D-44780 BOCHUM,GERMANY

来源：

YEAST | 1994年 / 10卷 / 12期

关键词：

PEROXISOME; YEAST; SACCHAROMYCES CEREVISIAE; SITE-DIRECTED MUTAGENESIS; AAA-FAMILY;

D O I：

10.1002/yea.320101210

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1613 / 1620

页数：8

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