TAILIEUCHUNG - Báo cáo khoa học: The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH

The folding of a 93-residue protein, the histidine-phospho-carrier protein ofStreptomyces coelicolor,HPr,hasbeen studied using several biophysical techniques, namely fluo-rescence, 8-anilinonaphthalene-1-sulfate binding, circular dichroism, Fourier transform infrared spectroscopy, gel filtration chromatography and differential scanning calori-metry. The chemical-denaturation behaviour of HPr, fol-lowed by fluorescence, CD and gel filtration, at pH and 25 C, is described as a two-state process, which does not involve the accumulation of thermodynamically stable intermediates. Its conformational stability under those con-ditions isDG¼ ± kcalÆmol )1 (1 kcal ¼), which makes the HPr fromS. coelicolorthe most unstable member of the HPr family described so far. . | Eur. J. Biochem. 270 2254-2267 2003 FEBS 2003 doi The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH Greaorio Fernandez-Ballester1. Javier Mava1 Alejandro Martin1 Stenhan Parche2 Javier Gomez1 Fritz Titgemeyer2 and Jose L. Neira1 3 1Instituto de Biologia Molecular y Celular Universidad Miguel Hernandez Elche Alicante Spain 2Lehrstuhl fur Mikrobiologie Friedrich-Alexander-Universitat Erlangen-Nurnberg Germany 3Instituto de Biocomputacion y Fisica de los sistemas complejos Zaragoza Spain The folding of a 93-residue protein the histidine-phospho-carrier protein of Streptomyces coelicolor HPr has been studied using several biophysical techniques namely fluorescence 8-anilinonaphthalene-1-sulfate binding circular dichroism Fourier transform infrared spectroscopy gel filtration chromatography and differential scanning calorimetry. The chemical-denaturation behaviour of HPr followed by fluorescence CD and gel filtration at pH and 25 C is described as a two-state process which does not involve the accumulation of thermodynamically stable intermediates. Its conformational stability under those conditions is AG kcal-mol-1 1 kcal k which makes the HPr from S. coelicolor the most unstable member of the HPr family described so far. The stability of the protein does not change significantly from pH 7-9 as concluded from the differential scanning calorimetry and thermal CD experiments. Conformational studies at low pH pH suggest that in the absence of cosmotropic agents HPr does not unfold completely rather it accumulates partially folded species. The transition from those species to other states with native-like secondary and tertiary structure occurs with a pKa as measured by the averaged measurements obtained by CD and fluorescence. However this transition does not agree either with a that measured by burial of hydrophobic patches .

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