Dissociation of the dimer of the intrinsically disordered domain of RNase Y upon antibody binding

Although RNase Y acts as the key enzyme initiating mRNA decay in Bacillus subtilis and likely in many other Gram positive bacteria, its three-dimensional structure remains unknown. An antibody, belonging to the rare IgG2b, λx isotype, was raised against a 12-residue conserved peptide from the N-terminal non-catalytic domain of Bacillus subtilis RNase Y (BsRNaseY) that is predicted to be intrinsically disordered. Here we show that this domain can be produced as a stand-alone protein called Nter-BsRNaseY that undergoes conformational changes between monomeric and dimeric forms.

https://ift.tt/2D5k9k5