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Int. J. Mol. Sci. 2018, 19(7), 1857; https://doi.org/10.3390/ijms19071857

The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties

1
Center for Environmental Biology and Chemistry Research, Facultad Experimental de Ciencias y Tecnología, Universidad de Carabobo, 2001 Valencia, Venezuela
2
Facultad de Farmacia, Departamento de Química Física II, Universidad Complutense de Madrid, 28040 Madrid, Spain
3
Instituto de Estructura de la Materia, IEM-CSIC, Serrano 121, 28006 Madrid, Spain
4
Department of Chemistry and Physics, Research Centre CIAIMBITAL, University of Almería- ceiA3, 04120 Almería, Spain
5
Department of Physical Chemistry, University of Murcia, 30003 Murcia, Spain
6
CNR-NANOTEC, Licryl-UOS Cosenza and CEMIF.Cal, Department of Physics, University of Calabria, 87036 Rende, Italy
7
Instituto de Bioquímica Vegetal y Fotosíntesis, CSIC-Universidad de Sevilla, 41092 Seville, Spain
8
Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, 03202 Elche (Alicante), Spain
9
Instituto de Biocomputación y Física de Sistemas Complejos, Joint Units IQFR-CSIC-BIFI, and GBsC-CSIC-BIFI, Universidad de Zaragoza, 50009 Zaragoza, Spain
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Received: 18 May 2018 / Revised: 18 June 2018 / Accepted: 20 June 2018 / Published: 24 June 2018
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Abstract

The LrtA protein of Synechocystis sp. PCC 6803 intervenes in cyanobacterial post-stress survival and in stabilizing 70S ribosomal particles. It belongs to the hibernating promoting factor (HPF) family of proteins, involved in protein synthesis. In this work, we studied the conformational preferences and stability of isolated LrtA in solution. At physiological conditions, as shown by hydrodynamic techniques, LrtA was involved in a self-association equilibrium. As indicated by Nuclear Magnetic Resonance (NMR), circular dichroism (CD) and fluorescence, the protein acquired a folded, native-like conformation between pH 6.0 and 9.0. However, that conformation was not very stable, as suggested by thermal and chemical denaturations followed by CD and fluorescence. Theoretical studies of its highly-charged sequence suggest that LrtA had a Janus sequence, with a context-dependent fold. Our modelling and molecular dynamics (MD) simulations indicate that the protein adopted the same fold observed in other members of the HPF family (β-α-β-β-β-α) at its N-terminal region (residues 1–100), whereas the C terminus (residues 100–197) appeared disordered and collapsed, supporting the overall percentage of overall secondary structure obtained by CD deconvolution. Then, LrtA has a chameleonic sequence and it is the first member of the HPF family involved in a self-association equilibrium, when isolated in solution. View Full-Text
Keywords: conformational plasticity; disordered protein; folding; ribosomal protein; spectroscopy; protein stability conformational plasticity; disordered protein; folding; ribosomal protein; spectroscopy; protein stability
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Contreras, L.M.; Sevilla, P.; Cámara-Artigas, A.; Hernández-Cifre, J.G.; Rizzuti, B.; Florencio, F.J.; Muro-Pastor, M.I.; García de la Torre, J.; Neira, J.L. The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties. Int. J. Mol. Sci. 2018, 19, 1857.

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