Disparate HDV ribozyme crystal structures represent intermediates on a rugged free-energy landscape

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F14%3A33152334" target="_blank" >RIV/61989592:15310/14:33152334 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/14:00431756 RIV/00216224:14740/14:00076675

Výsledek na webu

<a href="http://dx.doi.org/10.1261/rna.044982.114" target="_blank" >http://dx.doi.org/10.1261/rna.044982.114</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1261/rna.044982.114" target="_blank" >10.1261/rna.044982.114</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Disparate HDV ribozyme crystal structures represent intermediates on a rugged free-energy landscape

Popis výsledku v původním jazyce

The hepatitis delta virus (HDV) ribozyme is a member of the class of small, self-cleaving catalytic RNAs found in a wide range of genomes from HDV to human. Both pre- and post-catalysis (precursor and product) crystal structures of the cis-acting genomicHDV ribozyme have been determined. These structures, together with extensive solution probing, have suggested that a significant conformational change accompanies catalysis. A recent crystal structure of a trans-acting precursor, obtained at low pH andby molecular replacement from the previous product conformation, conforms to the product, raising the possibility that it represents an activated conformer past the conformational change. Here, using fluorescence resonance energy transfer (FRET), we discovered that cleavage of this ribozyme at physiological pH is accompanied by a structural lengthening in magnitude comparable to previous trans-acting HDV ribozymes. Conformational heterogeneity observed by FRET in solution appears to have

Název v anglickém jazyce

Disparate HDV ribozyme crystal structures represent intermediates on a rugged free-energy landscape

Popis výsledku anglicky

The hepatitis delta virus (HDV) ribozyme is a member of the class of small, self-cleaving catalytic RNAs found in a wide range of genomes from HDV to human. Both pre- and post-catalysis (precursor and product) crystal structures of the cis-acting genomicHDV ribozyme have been determined. These structures, together with extensive solution probing, have suggested that a significant conformational change accompanies catalysis. A recent crystal structure of a trans-acting precursor, obtained at low pH andby molecular replacement from the previous product conformation, conforms to the product, raising the possibility that it represents an activated conformer past the conformational change. Here, using fluorescence resonance energy transfer (FRET), we discovered that cleavage of this ribozyme at physiological pH is accompanied by a structural lengthening in magnitude comparable to previous trans-acting HDV ribozymes. Conformational heterogeneity observed by FRET in solution appears to have

Druh

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

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

—

Projekt

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

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

RNA-A Publication of the RNA Society

ISSN

1355-8382

e-ISSN

—

Svazek periodika

20

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

17

Strana od-do

1112-1128

Kód UT WoS článku

000338271200016

EID výsledku v databázi Scopus

—