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Oligomerization of a molecular chaperone modulates its activity.

Elife. 2018-05; 
SaioTomohide,KawagoeSoichiro,IshimoriKoichiro,KalodimosCharalamp
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Peptide Synthesis … recombinant DNA reagent TF Takara Bio inc. pCold-TF (TKR 3365) S7 S7 GenScript Gene synthesis peptide, recombinant protein GAPDH Sigma-Aldrich G-2267 software, algorithm CYANA3.97 Guntert 2004, Methods Mol Biol. PMID: 15318003 RRID:SCR_0 14229 … Get A Quote

摘要

Molecular chaperones alter the folding properties of cellular proteins via mechanisms that are not well understood. Here, we show that Trigger Factor (TF), an ATP-independent chaperone, exerts strikingly contrasting effects on the folding of non-native proteins as it transitions between a monomeric and a dimeric state. We used NMR spectroscopy to determine the atomic resolution structure of the 100 kDa dimeric TF. The structural data show that some of the substrate-binding sites are buried in the dimeric interface, explaining the lower affinity for protein substrates of the dimeric compared to the monomeric TF. Surprisingly, the dimeric TF associates faster with proteins and it exhibits stronger anti-... More

关键词

E. coli,NMR Spectroscopy,molecular biophysics,molecular chaperones,protein folding,structural bio
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