Local-to-global signal transduction at the core of a Mn2+ sensing riboswitch
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F19%3A00511789" target="_blank" >RIV/68081707:_____/19:00511789 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15310/19:73597473
Result on the web
<a href="https://www.nature.com/articles/s41467-019-12230-5.pdf" target="_blank" >https://www.nature.com/articles/s41467-019-12230-5.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-019-12230-5" target="_blank" >10.1038/s41467-019-12230-5</a>
Alternative languages
Result language
angličtina
Original language name
Local-to-global signal transduction at the core of a Mn2+ sensing riboswitch
Original language description
The widespread Mn2+-sensing yybP-ykoY riboswitch controls the expression of bacterial Mn2+ homeostasis genes. Here, we first determine the crystal structure of the ligand-bound yybP-ykoY riboswitch aptamer from Xanthomonas oryzae at 2.96 angstrom resolution, revealing two conformations with docked four-way junction (4WJ) and incompletely coordinated metal ions. In >100 mu s of MD simulations, we observe that loss of divalents from the core triggers local structural perturbations in the adjacent docking interface, laying the foundation for signal transduction to the regulatory switch helix. Using single-molecule FRET, we unveil a previously unobserved extended 4WJ conformation that samples transient docked states in the presence of Mg2+. Only upon adding sub-millimolar Mn2+, however, can the 4WJ dock stably, a feature lost upon mutation of an adenosine contacting Mn2+ in the core. These observations illuminate how subtly differing ligand preferences of competing metal ions become amplified by the coupling of local with global RNA dynamics.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10602 - Biology (theoretical, mathematical, thermal, cryobiology, biological rhythm), Evolutionary biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Communications
ISSN
2041-1723
e-ISSN
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Volume of the periodical
10
Issue of the periodical within the volume
SEP 20 2019
Country of publishing house
GB - UNITED KINGDOM
Number of pages
16
Pages from-to
4304
UT code for WoS article
000486995200014
EID of the result in the Scopus database
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