000124469 001__ 124469
000124469 005__ 20241125101202.0
000124469 0247_ $$2doi$$a10.1016/j.abb.2023.109538
000124469 0248_ $$2sideral$$a132867
000124469 037__ $$aART-2023-132867
000124469 041__ $$aeng
000124469 100__ $$aNeira, José L.
000124469 245__ $$aFolding of the nascent polypeptide chain of a histidine phosphocarrier protein in vitro
000124469 260__ $$c2023
000124469 5060_ $$aAccess copy available to the general public$$fUnrestricted
000124469 5203_ $$aThe phosphotransferase system (PTS), a metabolic pathway formed by five proteins, modulates the use of sugars in bacteria. The second protein in the chain is the histidine phosphocarrier, HPr, with the binding site at His15. The HPr kinase/phosphorylase (HPrK/P), involved in the bacterial use of carbon sources, phosphorylates HPr at Ser46, and it binds at its binding site. The regulator of sigma D protein (Rsd) also binds to HPr at His15. We have designed fragments of HPr, growing from its N-terminus and containing the His15. In this work, we obtained three fragments, HPr38, HPr58 and HPr70, comprising the first thirty-eight, fifty-eight and seventy residues of HPr, respectively. All fragments were mainly disordered, with evidence of a weak native-like, helical population around the binding site, as shown by fluorescence, far-ultraviolet circular dichroism, size exclusion chromatography and nuclear magnetic resonance. Although HPr38, HPr58 and HPr70 were disordered, they could bind to: (i) the N-terminal domain of first protein of the PTS, EIN; (ii) Rsd; and, (iii) HPrK/P, as shown by fluorescence and biolayer interferometry (BLI). The association constants for each protein to any of the fragments were in the low micromolar range, within the same range than those measured in the binding of HPr to each protein. Then, although acquisition of stable, native-like secondary and tertiary structures occurred at the last residues of the polypeptide, the ability to bind protein partners happened much earlier in the growing chain. Binding was related to the presence of the native-like structure around His15.
000124469 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000124469 590__ $$a3.8$$b2023
000124469 592__ $$a0.888$$b2023
000124469 591__ $$aBIOPHYSICS$$b15 / 77 = 0.195$$c2023$$dQ1$$eT1
000124469 593__ $$aBiophysics$$c2023$$dQ1
000124469 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b114 / 313 = 0.364$$c2023$$dQ2$$eT2
000124469 593__ $$aMolecular Biology$$c2023$$dQ2
000124469 593__ $$aBiochemistry$$c2023$$dQ2
000124469 594__ $$a7.4$$b2023
000124469 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000124469 700__ $$aPalomino-Schätzlein, Martina
000124469 773__ $$g736 (2023), 109538 [15 pp.]$$pArch. biochem. biophys.$$tARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS$$x0003-9861
000124469 8564_ $$s2013135$$uhttps://zaguan.unizar.es/record/124469/files/texto_completo.pdf$$yVersión publicada
000124469 8564_ $$s2594147$$uhttps://zaguan.unizar.es/record/124469/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000124469 909CO $$ooai:zaguan.unizar.es:124469$$particulos$$pdriver
000124469 951__ $$a2024-11-22-12:12:18
000124469 980__ $$aARTICLE