The structure of DarB in complex with RelNTD reveals nonribosomal activation of Rel stringent factors
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00567687" target="_blank" >RIV/61388963:_____/23:00567687 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22330/23:43926495
Result on the web
<a href="https://doi.org/10.1126/sciadv.ade4077" target="_blank" >https://doi.org/10.1126/sciadv.ade4077</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1126/sciadv.ade4077" target="_blank" >10.1126/sciadv.ade4077</a>
Alternative languages
Result language
angličtina
Original language name
The structure of DarB in complex with RelNTD reveals nonribosomal activation of Rel stringent factors
Original language description
Rel stringent factors are bifunctional ribosome-associated enzymes that catalyze both synthesis and hydrolysis of the alarmones (p)ppGpp. Besides the allosteric control by starved ribosomes and (p)ppGpp, Rel is regulated by various protein factors depending on specific stress conditions, including the c-di-AMP–binding protein DarB. However, how these effector proteins control Rel remains unknown. We have determined the crystal structure of the DarB2:RelNTD2 complex, uncovering that DarB directly engages the SYNTH domain of Rel to stimulate (p)ppGpp synthesis. This association with DarB promotes a SYNTH-primed conformation of the N-terminal domain region, markedly increasing the affinity of Rel for ATP while switching off the hydrolase activity of the enzyme. Binding to c-di-AMP rigidifies DarB, imposing an entropic penalty that precludes DarB-mediated control of Rel during normal growth. Our experiments provide the basis for understanding a previously unknown mechanism of allosteric regulation of Rel stringent factors independent of amino acid starvation.
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
10606 - Microbiology
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Science Advances
ISSN
2375-2548
e-ISSN
2375-2548
Volume of the periodical
9
Issue of the periodical within the volume
3
Country of publishing house
US - UNITED STATES
Number of pages
14
Pages from-to
eade4077
UT code for WoS article
000964550100003
EID of the result in the Scopus database
2-s2.0-85146485545