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

J 2013

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

PAPOUŠKOVÁ, Veronika; Pavel KADEŘÁVEK; Olga OTRUSINOVÁ; Alžběta RABATINOVÁ; Hana ŠANDEROVÁ et. al.

Základní údaje

Originální název

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

Autoři

PAPOUŠKOVÁ, Veronika (203 Česká republika, domácí); Pavel KADEŘÁVEK (203 Česká republika, domácí); Olga OTRUSINOVÁ (203 Česká republika, domácí); Alžběta RABATINOVÁ (203 Česká republika); Hana ŠANDEROVÁ (203 Česká republika); Jiří NOVÁČEK (203 Česká republika, domácí); Libor KRÁSNÝ (203 Česká republika); Vladimír SKLENÁŘ (203 Česká republika, domácí) a Lukáš ŽÍDEK (203 Česká republika, garant, domácí)

Vydání

ChemBioChem, WEINHEIM, WILEY-VCH Verlag, 2013, 1439-4227

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.060

Kód RIV

RIV/00216224:14740/13:00066324

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1002/cbic.201300226

UT WoS

000325851800012

Klíčová slova anglicky

NMR spectroscopy; RNA polymerase; partially disordered proteins; protein structures; delta subunit

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 4. 2014 08:42, Olga Křížová

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GA13-16842S, projekt VaV

Název: PODJEDNOTKY URČUJÍCÍ DNA SPECIFICITU BAKTERIÁLNÍ RNA POLYMERÁZY S FLEXIBILNÍMI DOMÉNAMI: FUNKCE A DYNAMIKA

Investor: Grantová agentura ČR, Podjednotky urcující DNA specificitu bakteriální RNA polymerázy s flexibilními doménami: funkce a dynamika

GA204/09/0583, projekt VaV

Název: Delta podjednotka RNA polymerázy z Gram pozitivních bakterií (Akronym: DELTA)

Investor: Grantová agentura ČR, Delta podjednotka RNA polymerázy z Gram pozitivních bakterií

Citovat

PAPOUŠKOVÁ, Veronika; Pavel KADEŘÁVEK; Olga OTRUSINOVÁ; Alžběta RABATINOVÁ; Hana ŠANDEROVÁ; Jiří NOVÁČEK; Libor KRÁSNÝ; Vladimír SKLENÁŘ a Lukáš ŽÍDEK. Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis. ChemBioChem. WEINHEIM: WILEY-VCH Verlag, 2013, roč. 14, č. 14, s. 1772-1779. ISSN 1439-4227. Dostupné z: https://dx.doi.org/10.1002/cbic.201300226.

@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 a 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, roč.~14, č.~14, s.~1772-1779. ISSN~1439-4227. Dostupné z: https://dx.doi.org/10.1002/cbic.201300226.

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