Do nucleic acids moonlight as molecular chaperones?

被引:47
作者
Docter, Brianne E. [1 ]
Horowitz, Scott [2 ,3 ]
Gray, Michael J. [2 ,4 ]
Jakob, Ursula [2 ]
Bardwell, James C. A. [1 ,2 ,3 ]
机构
[1] Univ Michigan, Cellular & Mol Biol Program, Ann Arbor, MI 48109 USA
[2] Univ Michigan, Dept Mol Cellular & Dev Biol, Ann Arbor, MI 48109 USA
[3] Univ Michigan, Howard Hughes Med Inst, Ann Arbor, MI 48109 USA
[4] Univ Alabama Birmingham, Dept Microbiol, Birmingham, AL 35294 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
RECOMBINANT PRION PROTEIN; HEAT-SHOCK PROTEINS; 23S RIBOSOMAL-RNA; STRESS GRANULES; MESSENGER-RNA; FOLDING ACTIVITY; DOMAIN-V; IN-VIVO; AGGREGATION; STABILITY;
D O I
10.1093/nar/gkw291
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
Organisms use molecular chaperones to combat the unfolding and aggregation of proteins. While protein chaperones have been widely studied, here we demonstrate that DNA and RNA exhibit potent chaperone activity in vitro. Nucleic acids suppress the aggregation of classic chaperone substrates up to 300-fold more effectively than the protein chaperone GroEL. Additionally, RNA cooperates with the DnaK chaperone system to refold purified luciferase. Our findings reveal a possible new role for nucleic acids within the cell: that nucleic acids directly participate in maintaining proteostasis by preventing protein aggregation.
引用
收藏
页码:4835 / 4845
页数:11
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