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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Bibliografiske detaljer
Udgivet i:J Biol Chem
Main Authors: Kishor, Aparna, White, Elizabeth J. F., Matsangos, Aerielle E., Yan, Zisui, Tandukar, Bishal, Wilson, Gerald M.
Format: Artigo
Sprog:Inglês
Udgivet: American Society for Biochemistry and Molecular Biology 2017
Fag:
RNA
Online adgang: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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