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线粒体前体蛋白与输入受体Tom70和Tom20的细胞质结构域的结合由细胞质伴侣蛋白决定。

Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors Tom70 and Tom20 is determined by cytoplasmic chaperones.

作者信息

Komiya T, Rospert S, Schatz G, Mihara K

机构信息

Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan.

出版信息

EMBO J. 1997 Jul 16;16(14):4267-75. doi: 10.1093/emboj/16.14.4267.

DOI:10.1093/emboj/16.14.4267
PMID:9250670
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1170052/
Abstract

We have reconstituted the early steps of precursor targeting to mitochondria in a defined and soluble system consisting of the cytosolic domains of the yeast mitochondrial import receptors Tom20 and Tom70, precursor to bovine adrenal adrenodoxin (which has a cleavable targeting signal) and rat liver cytosolic chaperones hsp70 and mitochondrial import-stimulating factor (MSF). The Tom70 domain only bound the precursor in the presence of MSF, yielding a precursor-MSF-Tom70 complex; ATP hydrolysis by MSF released MSF and generated a precursor-Tom70 complex whose formation was inhibited by an excess of a functional presequence peptide, but not by 150 mM NaCl. In the presence of the Tom20 domain, ATP caused transfer of the precursor from the precursor-MSF-Tom70 complex to Tom20. The Tom20 domain alone only bound the precursor in the presence of hsp70; hsp70 itself was not incorporated into the resulting complex. Formation of the Tom20-precursor complex was inhibited by excess presequence peptide or by 150 mM NaCl. Similar results were obtained with the ADP/ATP carrier and porin precursors, which both lack a cleaved targeting signal. Correct targeting of a precursor to mitochondrial import receptors thus requires cytosolic chaperones, irrespective of the presence or absence of a cleavable presequence.

摘要

我们在一个特定的可溶性系统中重构了前体靶向线粒体的早期步骤,该系统由酵母线粒体输入受体Tom20和Tom70的胞质结构域、牛肾上腺肾上腺皮质铁氧还蛋白前体(具有可裂解的靶向信号)以及大鼠肝脏胞质伴侣蛋白hsp70和线粒体输入刺激因子(MSF)组成。Tom70结构域仅在MSF存在时结合前体,产生前体-MSF-Tom70复合物;MSF水解ATP释放出MSF并生成前体-Tom70复合物,其形成受到过量功能性前序列肽的抑制,但不受150 mM NaCl的抑制。在Tom20结构域存在的情况下,ATP导致前体从前体-MSF-Tom70复合物转移到Tom20。单独的Tom20结构域仅在hsp70存在时结合前体;hsp70本身并未掺入形成的复合物中。Tom20-前体复合物的形成受到过量前序列肽或150 mM NaCl的抑制。对于ADP/ATP载体和孔蛋白前体也获得了类似的结果,它们都缺乏可裂解的靶向信号。因此,前体正确靶向线粒体输入受体需要胞质伴侣蛋白,而与是否存在可裂解的前序列无关。

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