Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole

被引:17
作者
Satyanarayana, C
Schröder-Köhne, S
Craig, EA
Schu, PV
Horst, M
机构
[1] Univ Gottingen, Biochem Abt 2, Inst Mol Zellbiol & Biochem, D-37073 Gottingen, Germany
[2] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany
[3] Univ Wisconsin, Sch Med, Dept Biomol Chem, Madison, WI 53706 USA
关键词
aminopeptidase; 1; heat shock protein 70; protein transport; vacuole; yeast;
D O I
10.1016/S0014-5793(00)01324-7
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
Eukaryotic 70 kDa heat shock proteins (Hsp70s) are localized in various cellular compartments and exhibit functions such as protein translocation across membranes, protein folding and assembly. Here we demonstrate that the constitutively expressed members of the yeast cytoplasmic Ssa subfamily, Ssa1/2p, are involved in the transport of the vacuolar hydrolase aminopeptidase I from the cytoplasm into the vacuole, The Ssap family members displayed overlapping functions in the transport of aminopeptidase 1, In SSAI and SSAII deletion mutants the precursor of aminopeptidase I accumulated in a dodecameric complex that is packaged in prevacuolar transport vesicles, Ssa1/2p was prominently localized to the vacuolar membrane, consistent with the role we propose for Ssa proteins in the fusion of transport vesicles with the vacuolar membrane. (C) 2000 Federation of European Biochemical Societies.
引用
收藏
页码:232 / 238
页数:7
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