The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer.
The 191-residue-long LrtA protein of Synechocystis sp. PCC 6803 is involved in post-stress survival and in stabilizing 70S ribosomal particles. It belongs to the hibernating promoting factor (HPF) family, intervening in protein synthesis. The protein consists of two domains: The N-terminal region (N-LrtA, residues 1⁻101), which is common to all the members of the HPF, and seems to be well-folded; and the C-terminal region (C-LrtA, residues 102⁻191), which is hypothesized to be disordered. In this work, we studied the conformational preferences of isolated C-LrtA in solution. The protein was disordered, as shown by computational modelling, 1D-¹H NMR, steady-state far-UV circular dichroism (CD) and chemical and thermal denaturations followed by fluorescence and far-UV CD. Moreover, at physiological conditions, as indicated by several biochemical and hydrodynamic techniques, isolated C-LrtA intervened in a self-association equilibrium, involving several oligomerization reactions. Thus, C-LrtA was an oligomeric disordered protein.
['Neira|José L|JL|0000-0002-4933-0428', 'Giudici|A Marcela|AM|', 'Hornos|Felipe|F|', 'Arbe|Arantxa|A|0000-0002-5137-4649', 'Rizzuti|Bruno|B|0000-0003-1110-764X']
D001426:Bacterial Proteins D064267:Intrinsically Disordered Proteins D008958:Models, Molecular D000072417:Protein Domains D055503:Protein Multimerization D012269:Ribosomal Proteins D046940:Synechococcus
oligomer disordered protein folding protein stability ribosomal protein