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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191385" target="_blank" >RIV/00216208:11310/13:10191385 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/13:00422985 RIV/00216224:14740/13:00066324

Výsledek na webu

<a href="http://dx.doi.org/10.1002/cbic.201300226" target="_blank" >http://dx.doi.org/10.1002/cbic.201300226</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/cbic.201300226" target="_blank" >10.1002/cbic.201300226</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 comparedto 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, transientcontacts 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 rela

Název v anglickém jazyce

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

Popis výsledku anglicky

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 comparedto 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, transientcontacts 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 rela

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Chembiochem : a European journal of chemical biology

ISSN

1439-4227

e-ISSN

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Svazek periodika

14

Číslo periodika v rámci svazku

14

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

1772-1779

Kód UT WoS článku

000325851800012

EID výsledku v databázi Scopus

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