Multitasking in the mitochondrion by the ATP-dependent Lon protease.
Multitasking in the mitochondrion by the ATP-dependent Lon protease.
复制标题
通过ATP依赖性LON蛋白酶在线粒体中的多任务。
DOI:
10.1016/j.bbamcr.2011.11.003
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发表时间:
2012-01
期刊:
影响因子:
--
通讯作者:
Suzuki CK
中科院分区:
文献类型:
--
作者:
Venkatesh S;Lee J;Singh K;Lee I;Suzuki CK
The AAA+ Lon protease is a soluble single-ringed homo-oligomer, which represents the most streamlined operational unit mediating ATP-dependent proteolysis. Despite its simplicity, the architecture of Lon proteases exhibits a species-specific diversity. Homology modeling provides insights into the structural features that distinguish bacterial and human Lon proteases as hexameric complexes from yeast Lon, which is uniquely heptameric. The best-understood functions of mitochondrial Lon are linked to maintaining proteostasis under normal metabolic conditions, and preventing proteotoxicity during environmental and cellular stress. An intriguing property of human Lon is its specific binding to G-quadruplex DNA, and its association with the mitochondrial genome in cultured cells. A fraction of Lon preferentially binds to the control region of mitochondrial DNA where transcription and replication are initiated. Here, we present an overview of the diverse functions of mitochondrial Lon, as well as speculative perspectives on its role in protein and mtDNA quality control.
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影响因子:
3.2
作者:
CHARETTE, MF;HENDERSON, GW;MARKOVITZ, A
通讯作者:
MARKOVITZ, A
影响因子:
3.5
作者:
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影响因子:
3.2
作者:
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通讯作者:
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影响因子:
11.8
作者:
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通讯作者:
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影响因子:
5.6
作者:
de Sagarra, MR;Mayo, I;Castaño, JG
通讯作者:
Castaño, JG