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- W2902179613 abstract "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 1101), 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." @default.
- W2902179613 created "2018-12-11" @default.
- W2902179613 creator A5021021363 @default.
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- W2902179613 date "2018-12-05" @default.
- W2902179613 modified "2023-10-15" @default.
- W2902179613 title "The C Terminus of the Ribosomal-Associated Protein LrtA is an Intrinsically Disordered Oligomer" @default.
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- W2902179613 doi "https://doi.org/10.3390/ijms19123902" @default.
- W2902179613 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6321479" @default.
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- W2902179613 hasPublicationYear "2018" @default.
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