Mostrar el registro sencillo del ítem
The Histidine Phosphocarrier Kinase/Phosphorylase from Bacillus Subtilis Is an Oligomer in Solution with a High Thermal Stability
dc.contributor.author | Neira, José L. | |
dc.contributor.author | Cámara Artigas, Ana | |
dc.contributor.author | Hernández Cifre, José Ginés | |
dc.contributor.author | Grazia Ortore, María | |
dc.date.accessioned | 2021-04-12T08:16:49Z | |
dc.date.available | 2021-04-12T08:16:49Z | |
dc.date.issued | 2021-03-22 | |
dc.identifier.issn | 1422-0067 | |
dc.identifier.uri | http://hdl.handle.net/10835/10487 | |
dc.description.abstract | The histidine phosphocarrier protein (HPr) kinase/phosphorylase (HPrK/P) modulates the phosphorylation state of the HPr protein, and it is involved in the use of carbon sources by Gram-positive bacteria. Its X-ray structure, as concluded from crystals of proteins from several species, is a hexamer; however, there are no studies about its conformational stability, and how its structure is modified by the pH. We have embarked on the conformational characterization of HPrK/P of Bacillus subtilis (bsHPrK/P) in solution by using several spectroscopic (namely, fluorescence and circular dichroism (CD)) and biophysical techniques (namely, small-angle X-ray-scattering (SAXS) and dynamic light-scattering (DLS)). bsHPrK/P was mainly a hexamer in solution at pH 7.0, in the presence of phosphate. The protein had a high conformational stability, with an apparent thermal denaturation midpoint of ~70 °C, at pH 7.0, as monitored by fluorescence and CD. The protein was very pH-sensitive, precipitated between pH 3.5 and 6.5; below pH 3.5, it had a molten-globule-like conformation; and it acquired a native-like structure in a narrow pH range (between pH 7.0 and 8.0). Guanidinium hydrochloride (GdmCl) denaturation occurred through an oligomeric intermediate. On the other hand, urea denaturation occurred as a single transition, in the range of concentrations between 1.8 and 18 µM, as detected by far-UV CD and fluorescence. | es_ES |
dc.language.iso | en | es_ES |
dc.publisher | MDPI | es_ES |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | circular dichroism | es_ES |
dc.subject | conformational stability | es_ES |
dc.subject | fluorescence | es_ES |
dc.subject | phosphorylation | es_ES |
dc.title | The Histidine Phosphocarrier Kinase/Phosphorylase from Bacillus Subtilis Is an Oligomer in Solution with a High Thermal Stability | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.relation.publisherversion | https://www.mdpi.com/1422-0067/22/6/3231 | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es_ES |
dc.identifier.doi | https://doi.org/10.3390/ijms22063231 |