dc.creator | Contreras, Lellys M. | es |
dc.creator | Sevilla, Paz | es |
dc.creator | Cámara Artigas, Ana | es |
dc.creator | Hernández Cifre, José G. | es |
dc.creator | Rizzuti, Bruno | es |
dc.creator | Florencio Bellido, Francisco Javier | es |
dc.creator | Muro Pastor, María Isabel | es |
dc.creator | García de la Torre, José | es |
dc.creator | Neira, José L. | es |
dc.date.accessioned | 2018-08-06T08:04:05Z | |
dc.date.available | 2018-08-06T08:04:05Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Contreras, L.M., Sevilla, P., Cámara Artigas, A., Hernández Cifre, J.G., Rizzuti, B., Florencio Bellido, F.J.,...,Neira, J.L. (2018). The cyanobacterial ribosomal-associated protein LrtA from Synechocystis sp. PCC 6803 is an oligomeric protein in solution with chameleonic sequence properties. International Journal o f Molecular Sciences, 19 (7), 1857-1-1857-21. | |
dc.identifier.issn | 1422-0067 | es |
dc.identifier.uri | https://hdl.handle.net/11441/77839 | |
dc.description.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 ( - - - - - ) 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 |
dc.description.sponsorship | Ministerio de Economía y Competitividad CTQ2015-64445-R | es |
dc.description.sponsorship | Ministerio de Economía y Competitividad BIO2016-78020-R | es |
dc.description.sponsorship | Ministerio de Economía y Competitividad FIS2014-52212-R | es |
dc.description.sponsorship | Ministerio de Economía y Competitividad BIO2016-75634-P | es |
dc.description.sponsorship | Fundación Séneca 19353/PI/14 | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | MDPI | es |
dc.relation.ispartof | International Journal o f Molecular Sciences, 19 (7), 1857-1-1857-21. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Conformational plasticity | es |
dc.subject | Disordered protein | es |
dc.subject | Folding | es |
dc.subject | Ribosomal protein | es |
dc.subject | Spectroscopy | es |
dc.subject | Protein stability | es |
dc.title | The cyanobacterial ribosomal-associated protein LrtA from Synechocystis sp. PCC 6803 is an oligomeric protein in solution with chameleonic sequence properties | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Instituto de Bioquímica Vegetal y Fotosíntesis IBVF – CIC Cartuja | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | |
dc.relation.projectID | CTQ2015-64445-R | es |
dc.relation.projectID | BIO2016-78020-R | es |
dc.relation.projectID | FIS2014-52212-R | es |
dc.relation.projectID | BIO2016-75634-P | es |
dc.relation.projectID | 19353/PI/14 | es |
dc.relation.publisherversion | https://doi.org/10.3390/ijms19071857 | es |
dc.identifier.doi | 10.3390/ijms19071857 | es |
idus.format.extent | 21 p. | es |
dc.journaltitle | International Journal o f Molecular Sciences | es |
dc.publication.volumen | 19 | es |
dc.publication.issue | 7 | es |
dc.publication.initialPage | 1857-1 | es |
dc.publication.endPage | 1857-21 | es |