| PAPOUŠKOVÁ, Veronika, Pavel KADEŘÁVEK, Olga OTRUSINOVÁ, Alžběta RABATINOVÁ, Hana ŠANDEROVÁ, Jiří NOVÁČEK, Libor KRÁSNÝ, Vladimír SKLENÁŘ and Lukáš ŽÍDEK. Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis. ChemBioChem. WEINHEIM: WILEY-VCH Verlag, 2013, vol. 14, No 14, p. 1772-1779. ISSN 1439-4227. Available from: https://dx.doi.org/10.1002/cbic.201300226. |
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@article{1122510,
author = {Papoušková, Veronika and Kadeřávek, Pavel and Otrusinová, Olga and Rabatinová, Alžběta and Šanderová, Hana and Nováček, Jiří and Krásný, Libor and Sklenář, Vladimír and Žídek, Lukáš},
article_location = {WEINHEIM},
article_number = {14},
doi = {http://dx.doi.org/10.1002/cbic.201300226},
keywords = {NMR spectroscopy; RNA polymerase; partially disordered proteins; protein structures; delta subunit},
language = {eng},
issn = {1439-4227},
journal = {ChemBioChem},
title = {Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis},
url = {http://www.ncbi.nlm.nih.gov/pubmed/23868186},
volume = {14},
year = {2013}
}
TY - JOUR
ID - 1122510
AU - Papoušková, Veronika - Kadeřávek, Pavel - Otrusinová, Olga - Rabatinová, Alžběta - Šanderová, Hana - Nováček, Jiří - Krásný, Libor - Sklenář, Vladimír - Žídek, Lukáš
PY - 2013
TI - Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis
JF - ChemBioChem
VL - 14
IS - 14
SP - 1772-1779
EP - 1772-1779
PB - WILEY-VCH Verlag
SN - 14394227
KW - NMR spectroscopy
KW - RNA polymerase
KW - partially disordered proteins
KW - protein structures
KW - delta subunit
UR - http://www.ncbi.nlm.nih.gov/pubmed/23868186
L2 - http://www.ncbi.nlm.nih.gov/pubmed/23868186
N2 - 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.
ER -
PAPOUŠKOVÁ, Veronika, Pavel KADEŘÁVEK, Olga OTRUSINOVÁ, Alžběta RABATINOVÁ, Hana ŠANDEROVÁ, Jiří NOVÁČEK, Libor KRÁSNÝ, Vladimír SKLENÁŘ and Lukáš ŽÍDEK. Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis. \textit{ChemBioChem}. WEINHEIM: WILEY-VCH Verlag, 2013, vol.~14, No~14, p.~1772-1779. ISSN~1439-4227. Available from: https://dx.doi.org/10.1002/cbic.201300226.
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