Další formáty:
BibTeX
LaTeX
RIS
@article{1199998,
author = {Panecka, Joanna and Havrila, Marek and Réblová, Kamila and Šponer, Jiří and Trylska, Joanna},
article_location = {WASHINGTON},
article_number = {24},
doi = {http://dx.doi.org/10.1021/jp5030685},
keywords = {NUCLEIC-ACIDS; DECODING SITE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; RNA STRUCTURE; MINOR MOTIF; FORCE-FIELD; BASE-PAIRS; BINDING; SUBUNIT},
language = {eng},
issn = {1520-6106},
journal = {Journal of Physical Chemistry B},
title = {Role of S-turn2 in the Structure, Dynamics, and Function of Mitochondrial Ribosomal A-Site. A Bioinformatics and Molecular Dynamics Simulation Study},
url = {http://pubs.acs.org/doi/abs/10.1021/jp5030685},
volume = {118},
year = {2014}
}
TY - JOUR
ID - 1199998
AU - Panecka, Joanna - Havrila, Marek - Réblová, Kamila - Šponer, Jiří - Trylska, Joanna
PY - 2014
TI - Role of S-turn2 in the Structure, Dynamics, and Function of Mitochondrial Ribosomal A-Site. A Bioinformatics and Molecular Dynamics Simulation Study
JF - Journal of Physical Chemistry B
VL - 118
IS - 24
SP - 6687-6701
EP - 6687-6701
PB - American Chemical Society
SN - 15206106
KW - NUCLEIC-ACIDS
KW - DECODING SITE
KW - CRYSTAL-STRUCTURE
KW - ESCHERICHIA-COLI
KW - RNA STRUCTURE
KW - MINOR MOTIF
KW - FORCE-FIELD
KW - BASE-PAIRS
KW - BINDING
KW - SUBUNIT
UR - http://pubs.acs.org/doi/abs/10.1021/jp5030685
L2 - http://pubs.acs.org/doi/abs/10.1021/jp5030685
N2 - The mRNA decoding site (A-site) in the small ribosomal subunit controls fidelity of the translation process. Here, using molecular dynamics simulations and bioinformatic analyses, we investigated the structural dynamics of the human mitochondrial A-site (native and A1490G mutant) and compared it with the dynamics of the bacterial A-site. We detected and characterized a specific RNA backbone configuration, S-turn2, which occurs in the human mitochondrial but not in the bacterial A-site. Mitochondrial and bacterial A-sites show different propensities to form S-turn2 that may be caused by different base-pairing patterns of the flanking nucleotides. Also, the S-tum2 structural stability observed in the simulations supports higher accuracy and lower speed of mRNA decoding in mitochondria in comparison with bacteria. In the mitochondrial A-site, we observed collective movement of stacked nucleotides A1408 center dot C1409 center dot C1410, which may explain the known differences in aminoglycoside antibiotic binding affinities toward the studied A-site variants.
ER -
PANECKA, Joanna, Marek HAVRILA, Kamila RÉBLOVÁ, Jiří ŠPONER a Joanna TRYLSKA. Role of S-turn2 in the Structure, Dynamics, and Function of Mitochondrial Ribosomal A-Site. A Bioinformatics and Molecular Dynamics Simulation Study. \textit{Journal of Physical Chemistry B}. WASHINGTON: American Chemical Society, roč.~118, č.~24, s.~6687-6701. ISSN~1520-6106. doi:10.1021/jp5030685. 2014.
|
