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 of select mRNAs and has recently been shown to bind and stabilize some ARE-containing transcripts in cells. Previous studies indicated that both the ATP- and peptide-binding domains of Hsp70 contributed to the stability of Hsp70-RNA complexes and that ATP might inhibit RNA recruitment. This suggested the possibility that RNA binding by Hsp70 might mimic features of its peptide-directed chaperone activities. Here, using purified, cofactor-free preparations of recombinant human Hsp70 and quantitative biochemical approaches, we found that high-affinity RNA binding requires at least 30 nucleotides of RNA sequence but is independent of Hsp70's nucleotide-bound status, ATPase activity, or peptide-binding roles. Furthermore, although both the ATP- and peptide-binding domains of Hsp70 could form complexes with an ARE sequence from mRNA, only the peptide-binding domain could recover cellular mRNA in ribonucleoprotein immunoprecipitations. Finally, Hsp70-directed stabilization of mRNA in cells was mediated exclusively by the protein's peptide-binding domain. Together, these findings indicate that the RNA-binding and mRNA-stabilizing functions of Hsp70 are independent of its protein chaperone cycle but also provide potential mechanical explanations for several well-established and recently discovered cytoprotective and RNA-based Hsp70 functions.

As bacteria aggregate and form biofilms on surfaces in the human body such as tissues, indwelling medical devices, dressings and implants, they can cause a significant health risk. Bacterial biofilms possess altered phenotypes: physical features that facilitate antibiotic resistance and evasion of the host immune response. Since metabolic and physical factors contribute to biofilm maturation and persistence, an objective in antibiofilm therapy is to target these factors to deliver innovative approaches for solving these important health problems. Currently, there is little research on the direct immunological effects resulting from the introduction of foreign components to the body pertaining to biofilm inhibition methods. Detailed research involving animal models is necessary to better understand the biological side effects of synthetic peptides, genetically modified bacteriophages and isolated proteins and any resistance that may develop from these approaches. • D-Met, D-Phe and D-Trp enhance antibiotic activity (Sanchez et al. 2014) Peptides • Peptide 1018 suppresses expression of antibiotic resistance genes (Reffuveille et al.