Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis

0422985 - MBÚ 2014 RIV DE eng J - Článek v odborném periodiku
Papoušková, V. - Kadeřávek, P. - Otrusinová, O. - Rabatinová, Alžběta - Šanderová, Hana - Nováček, J. - Krásný, Libor - Sklenář, V. - Žídek, L.
Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis.
Chembiochem. Roč. 14, č. 14 (2013), s. 1772-1779. ISSN 1439-4227. E-ISSN 1439-7633
Grant CEP: GA ČR GA204/09/0583; GA ČR GA13-16842S
Institucionální podpora: RVO:61388971
Klíčová slova: NMR spectroscopy * partially disordered proteins * protein structures
Kód oboru RIV: CE - Biochemie
Impakt faktor: 3.060, rok: 2013

The partially disordered delta subunit of RNA polymerase was studied by various NMR techniques. The structure of the well-folded N-terminal domain was determined based on inter-proton distances in NOESY spectra. The obtained structural model was compared to the previously determined structure of a truncated construct (lacking the C-terminal domain). Only marginal differences were identified, thus indicating that the first structural model was not significantly compromised by the absence of the C-terminal domain. Various N-15 relaxation experiments were employed to describe the flexibility of both domains. The relaxation data revealed that the C-terminal domain is more flexible, but its flexibility is not uniform. By using paramagnetic labels, transient contacts of the C-terminal tail with the N-terminal domain and with itself were identified. A propensity of the C-terminal domain to form beta-type structures was obtained by chemical shift analysis. Comparison with the paramagnetic relaxation enhancement indicated a well-balanced interplay of repulsive and attractive electrostatic interactions governing the conformational behavior of the C-terminal domain. The results showed that the delta subunit consists of a well-ordered N-terminal domain and a flexible C-terminal domain that exhibits a complex hierarchy of partial ordering
Trvalý link: http://hdl.handle.net/11104/0229093