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Título: | Effect of phosphorylation in the structural behavior of peptides derived from the intrinsically disordered Cterminal domain of Histone H1.0 |
Autor: | Chaves-Arquero, Belén CSIC ORCID; Pérez Cañadillas, José Manuel CSIC ORCID ; Jiménez, M. Angeles CSIC ORCID | Palabras clave: | NMR spectroscopy Peptides Protein models Proteinstructures Phosphorylation Structure elucidation |
Fecha de publicación: | 21-abr-2020 | Editor: | Wiley-VCH | Citación: | Chemistry - a European Journal 26: 5970–5981 (2020) | Resumen: | o investigate the structural impact of phosphory-lation on the human histone H1.0 C-terminal domain,weperformed NMR structural studies of model peptides con-taining asingle phosphorylation site:T118-H1.0 (T118PKKmotif) andT140-H1.0 (T140PVK motif). Both model peptides aremainly disordered in aqueous solution in their non-phos-phorylated and phosphorylated forms, but become struc-tured in the presence of trifluoroethanol. The peptides T118-H1.0 and pT118-H1.0 contain two helical regions, along am-phipathic a helix spanning residues 104–115 and ashort a/310helix (residues 119–123),that are almostperpendicular inT118-H1.0 but have apoorly defined orientation in pT118-H1.0.Peptides T140-H1.0 and pT140-H1.0 form very similar a helicesbetween residues 141–147. The TPKK and TPVK motifs showthe same backbone conformation,but differ in their side-chain contacts;the Thr and pThr side chains interact withthe i + 2Lys side chain in the TPKK motif, andwith the i+ 3Lysside chain in the TPVK motif. The pT phosphate group inpT118-H1.0andpT140-H1.0haspKavaluesbelowtheintrinsicvalues, which can be explained by non-specific charge–chargeinteractions with nearbyLys. The non-polar ValintheTPVK motif accounts forthe pT140pKabeing closer to the in-trinsic pKavalue than the pT118pKa.Altogether,these resultsvalidate that minimalist strategies using model peptides canprovide structural details difficult to obtain in short-lived in-trinsically disordered proteins and domains. | Descripción: | 12 pags., 7 figs., 3 tabs. | Versión del editor: | https://doi.org/10.1002/chem.201905496 | URI: | http://hdl.handle.net/10261/220103 | DOI: | 10.1002/chem.201905496 | ISSN: | 0947-6539 | E-ISSN: | 1521-3765 |
Aparece en las colecciones: | (IQF) Artículos |
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2020_ChemEurJ_revisedversion_majimenez.pdf | Copia de autor | 1,87 MB | Adobe PDF | Visualizar/Abrir |
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