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Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions
Hsp70 is a protein chaperone that prevents protein aggregation and aids protein folding by binding to hydrophobic peptide domains through a reversible mechanism directed by an ATPase cycle. However, Hsp70 also binds U-rich RNA including some AU-rich elements (AREs) that regulate the decay kinetics o...
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| Pubblicato in: | J Biol Chem |
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| Autori principali: | , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Biochemistry and Molecular Biology
2017
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5572911/ https://ncbi.nlm.nih.gov/pubmed/28679534 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M117.785394 |
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