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- Title
The TFE-induced transient native-like structure of the intrinsically disordered $$\varvec\sigma_{ 4}^{ 70}$$ domain of Escherichia coli RNA polymerase.
- Authors
Kaczka, Piotr; Winiewska, Maria; Zhukov, Igor; Rempoła, Bożenna; Bolewska, Krystyna; Łoziński, Tomasz; Ejchart, Andrzej; Poznańska, Anna; Wierzchowski, Kazimierz; Poznański, Jarosław
- Abstract
The transient folding of domain 4 of an E. coli RNA polymerase $$\sigma^{70}$$ subunit ( $$r{\text{EC}}\sigma_{4}^{70}$$ ) induced by an increasing concentration of 2,2,2-trifluoroethanol (TFE) in an aqueous solution was monitored by means of CD and heteronuclear NMR spectroscopy. NMR data, collected at a 30 % TFE, allowed the estimation of the population of a locally folded $$r{\text{EC}}\sigma_{4}^{70}$$ structure (CSI descriptors) and of local backbone dynamics (N relaxation). The spontaneous organization of the helical regions of the initially unfolded protein into a TFE-induced 3D structure was revealed from structural constraints deduced from N- to C-edited NOESY spectra. In accordance with all the applied criteria, three highly populated α-helical regions, separated by much more flexible fragments, form a transient HLHTH motif resembling those found in PDB structures resolved for homologous proteins. All the data taken together demonstrate that TFE induces a transient native-like structure in the intrinsically disordered protein.
- Subjects
FLUOROETHANOL; RNA polymerases; ESCHERICHIA coli enzymes; PROTEIN folding; AQUEOUS solutions; NUCLEAR magnetic resonance spectroscopy; PROTEIN structure
- Publication
European Biophysics Journal, 2014, Vol 43, Issue 12, p581
- ISSN
0175-7571
- Publication type
Article
- DOI
10.1007/s00249-014-0987-4