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热休克蛋白100/Clp蛋白:一种共同机制解释多种功能。

HSP100/Clp proteins: a common mechanism explains diverse functions.

作者信息

Schirmer E C, Glover J R, Singer M A, Lindquist S

机构信息

Howard Hughes Medical Institute, Chicago, IL, USA.

出版信息

Trends Biochem Sci. 1996 Aug;21(8):289-96.

PMID:8772382
Abstract

The HSP100/Clp proteins are a newly discovered family with a great diversity of functions, such as increased tolerance to high temperatures, promotion of proteolysis of specific cellular substrates and regulation of transcription. HSP100/Clp proteins are also synthesized in a variety of specific patterns and, in eukaryotes, are localized to different subcellular compartments. Recent data suggest that a common ability to disassemble higher-order protein structures and aggregates unifies the molecular functions of this diverse family.

摘要

热休克蛋白100/Clp蛋白是一个新发现的家族,具有多种功能,如提高对高温的耐受性、促进特定细胞底物的蛋白质水解以及调节转录。热休克蛋白100/Clp蛋白也以多种特定模式合成,在真核生物中,定位于不同的亚细胞区室。最近的数据表明,拆解高阶蛋白质结构和聚集体的共同能力统一了这个多样家族的分子功能。

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Trends Biochem Sci. 1996 Aug;21(8):289-96.
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Protein binding and disruption by Clp/Hsp100 chaperones.蛋白质结合以及被Clp/Hsp100伴侣蛋白破坏。
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