The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties
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...
| Main Authors: | , , , , , , , , |
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| Format: | info:eu-repo/semantics/article |
| Language: | English |
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MDPI
2020
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| Subjects: | |
| Online Access: | http://hdl.handle.net/10835/7439 |
| _version_ | 1789406688056442880 |
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| author | Contreras, Lellys M. Sevilla, Paz Cámara Artigas, Ana María Hernández Cifre, José G. Rizzuti, Bruno Florencio, Francisco J. Muro Pastor, María Isabel García de la Torre, José Neira Faleiro, José Luis |
| author_facet | Contreras, Lellys M. Sevilla, Paz Cámara Artigas, Ana María Hernández Cifre, José G. Rizzuti, Bruno Florencio, Francisco J. Muro Pastor, María Isabel García de la Torre, José Neira Faleiro, José Luis |
| author_sort | Contreras, Lellys M. |
| collection | DSpace |
| description | 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. |
| format | info:eu-repo/semantics/article |
| id | oai:repositorio.ual.es:10835-7439 |
| institution | Universidad de Cuenca |
| language | English |
| publishDate | 2020 |
| publisher | MDPI |
| record_format | dspace |
| spelling | oai:repositorio.ual.es:10835-74392023-04-12T19:48:06Z The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties Contreras, Lellys M. Sevilla, Paz Cámara Artigas, Ana María Hernández Cifre, José G. Rizzuti, Bruno Florencio, Francisco J. Muro Pastor, María Isabel García de la Torre, José Neira Faleiro, José Luis conformational plasticity disordered protein folding ribosomal protein spectroscopy protein stability 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. 2020-01-16T12:56:39Z 2020-01-16T12:56:39Z 2018-06-24 info:eu-repo/semantics/article 1422-0067 http://hdl.handle.net/10835/7439 en https://www.mdpi.com/1422-0067/19/7/1857 Attribution-NonCommercial-NoDerivatives 4.0 Internacional http://creativecommons.org/licenses/by-nc-nd/4.0/ info:eu-repo/semantics/openAccess MDPI |
| spellingShingle | conformational plasticity disordered protein folding ribosomal protein spectroscopy protein stability Contreras, Lellys M. Sevilla, Paz Cámara Artigas, Ana María Hernández Cifre, José G. Rizzuti, Bruno Florencio, Francisco J. Muro Pastor, María Isabel García de la Torre, José Neira Faleiro, José Luis The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties |
| title | The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties |
| title_full | The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties |
| title_fullStr | The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties |
| title_full_unstemmed | The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties |
| title_short | The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties |
| title_sort | cyanobacterial ribosomal-associated protein lrta from synechocystis sp. pcc 6803 is an oligomeric protein in solution with chameleonic sequence properties |
| topic | conformational plasticity disordered protein folding ribosomal protein spectroscopy protein stability |
| url | http://hdl.handle.net/10835/7439 |
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