dc.contributor.author | Neira Faleiro, José Luis | |
dc.contributor.author | Giudici Besseghini, Ana Marcela | |
dc.contributor.author | Hornos Adán, Felipe | |
dc.contributor.author | Arbe Méndez, María Aranzazu | |
dc.contributor.author | Rizzuti, Bruno | |
dc.date.accessioned | 2019-03-05T18:32:11Z | |
dc.date.available | 2019-03-05T18:32:11Z | |
dc.date.issued | 2018-12-05 | |
dc.identifier.citation | International Journal Of Molecular Sciences 13(5) : (2018) // Article ID 3902 | es_ES |
dc.identifier.issn | 1422-0067 | |
dc.identifier.uri | http://hdl.handle.net/10810/31871 | |
dc.description.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 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-H-1 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. | es_ES |
dc.description.sponsorship | This research was funded by Spanish Ministry of Economy and Competitiveness [CTQ2015-64445-R (to J.L.N.) and MAT2015-63704-P (to A.A.), with Fondo Social Europeo (ESF)], and by the Basque Government [IT-654-13 (to A.A.)] | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | MDPI | es_ES |
dc.relation | info:eu-repo/grantAgreement/MINECO/CTQ2015-64445-R | es_ES |
dc.relation | info:eu-repo/grantAgreement/MINECO/MAT2015-63704-P | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.subject | disordered protein | es_ES |
dc.subject | folding | es_ES |
dc.subject | oligomer | es_ES |
dc.subject | ribosomal protein | es_ES |
dc.subject | protein stability | es_ES |
dc.subject | blue native electrophoresis | es_ES |
dc.subject | secondary structure analyses | es_ES |
dc.subject | light-repressed transcript | es_ES |
dc.subject | cytoplasmic domain | es_ES |
dc.subject | binding | es_ES |
dc.subject | complexes | es_ES |
dc.subject | determinants | es_ES |
dc.subject | spectroscopy | es_ES |
dc.subject | inhibitor | es_ES |
dc.subject | dynamics | es_ES |
dc.title | The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.relation.publisherversion | https://www.mdpi.com/1422-0067/19/12/3902 | es_ES |
dc.identifier.doi | 10.3390/ijms19123902 | |
dc.departamentoes | Física de materiales | es_ES |
dc.departamentoeu | Materialen fisika | es_ES |