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dc.contributor.authorContreras, Lellys M.
dc.contributor.authorSevilla, Paz
dc.contributor.authorCámara Artigas, Ana María
dc.contributor.authorHernández Cifre, José G.
dc.contributor.authorRizzuti, Bruno
dc.contributor.authorFlorencio, Francisco J.
dc.contributor.authorMuro Pastor, María Isabel
dc.contributor.authorGarcía de la Torre, José
dc.contributor.authorNeira Faleiro, José Luis
dc.date.accessioned2020-01-16T12:56:39Z
dc.date.available2020-01-16T12:56:39Z
dc.date.issued2018-06-24
dc.identifier.issn1422-0067
dc.identifier.urihttp://hdl.handle.net/10835/7439
dc.description.abstractThe 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.es_ES
dc.language.isoenes_ES
dc.publisherMDPIes_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectconformational plasticityes_ES
dc.subjectdisordered proteines_ES
dc.subjectfoldinges_ES
dc.subjectribosomal proteines_ES
dc.subjectspectroscopyes_ES
dc.subjectprotein stabilityes_ES
dc.titleThe Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Propertieses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherversionhttps://www.mdpi.com/1422-0067/19/7/1857es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivatives 4.0 Internacional