biostudies-literatureYang SWMinistry of Agriculture, Food and Rural Affairs2658-2675https://www.ebi.ac.uk/biostudies/studies/S-EPMC5901386biostudies-literatureUnknown32(5)A novel protein-folding function of RNA has been recognized, which can outperform previously known molecular chaperone proteins. The RNA as a molecular chaperone (chaperna) activity is intrinsic to some ribozymes and is operational during viral infections. Our purpose was to test whether influenza hemagglutinin (HA) can be assembled in a soluble, trimeric, and immunologically activating conformation by means of an RNA molecular chaperone (chaperna) activity. An RNA-interacting domain (RID) from the host being immunized was selected as a docking tag for RNA binding, which served as a transducer for the chaperna function for de novo folding and trimeric assembly of RID-HA1. Mutations that affect tRNA binding greatly increased the soluble aggregation defective in trimer assembly, suggesting tFASEB journal : official publication of the Federation of American Societies for Experimental BiologyHarnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.PMC5901386716002‐7Choi SIKwon SBByun YHSeong BLLee YJChae WKim CKYang SWKim PPark CKim YSJang YHfalseHarnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.A novel protein-folding function of RNA has been recognized, which can outperform previously known molecular chaperone proteins. The RNA as a molecular chaperone (chaperna) activity is intrinsic to some ribozymes and is operational during viral infections. Our purpose was to test whether influenza hemagglutinin (HA) can be assembled in a soluble, trimeric, and immunologically activating conformation by means of an RNA molecular chaperone (chaperna) activity. An RNA-interacting domain (RID) from the host being immunized was selected as a docking tag for RNA binding, which served as a transducer for the chaperna function for de novo folding and trimeric assembly of RID-HA1. Mutations that affect tRNA binding greatly increased the soluble aggregation defective in trimer assembly, suggesting t2018-01-01T00:00:00Z2018 May2026-04-30T18:54:50.729Z2019-03-26T23:45:40ZS-EPMC59013862929586410.1096/fj.201700747RR