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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