Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon

被引:138
作者
Rep, M
vanDijl, JM
Suda, K
Schatz, G
Grivell, LA
Suzuki, CK
机构
[1] UNIV BASEL,BIOZENTRUM,BIOCHEM ABT,CH-4056 BASEL,SWITZERLAND
[2] UNIV AMSTERDAM,DEPT MOL CELL BIOL,MOL BIOL SECT,NL-1098 SM AMSTERDAM,NETHERLANDS
关键词
D O I
10.1126/science.274.5284.103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria. Cells lacking both proteins exhibit defects in respiration-dependent growth, degradation of mitochondrially synthesized proteins, and assembly of inner-membrane complexes. Defects in growth and protein assembly, but not in degradation, were suppressed by overproduction of yeast mitochondrial Lon, an ATP-dependent serine protease. Suppression by Lon was enhanced by inactivation of the proteolytic site and was prevented by mutation of the ATP-binding site. It is suggested that the mitochondrial proteases Lon, Afg3p, and Rca1p can also serve a chaperone-like function in the assembly of mitochondrial protein complexes.
引用
收藏
页码:103 / 106
页数:4
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