Publication details

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

Authors

PAPOUŠKOVÁ Veronika KADEŘÁVEK Pavel OTRUSINOVÁ Olga RABATINOVÁ Alžběta ŠANDEROVÁ Hana NOVÁČEK Jiří KRÁSNÝ Libor SKLENÁŘ Vladimír ŽÍDEK Lukáš

Year of publication 2013
Type Article in Periodical
Magazine / Source ChemBioChem
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://www.ncbi.nlm.nih.gov/pubmed/23868186
Doi http://dx.doi.org/10.1002/cbic.201300226
Field Biochemistry
Keywords NMR spectroscopy; RNA polymerase; partially disordered proteins; protein structures; delta subunit
Description 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 15 N 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.
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