A monomer-dimer switch modulates the activity of plant adenosine kinase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F25%3A00639003" target="_blank" >RIV/61389030:_____/25:00639003 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15310/25:73630460 RIV/00216224:90242/25:00143938
Result on the web
<a href="https://doi.org/10.1093/jxb/eraf094" target="_blank" >https://doi.org/10.1093/jxb/eraf094</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/jxb/eraf094" target="_blank" >10.1093/jxb/eraf094</a>
Alternative languages
Result language
angličtina
Original language name
A monomer-dimer switch modulates the activity of plant adenosine kinase
Original language description
Adenosine undergoes ATP-dependent phosphorylation catalyzed by adenosine kinase (ADK). In plants, ADK also phosphorylates cytokinin ribosides, transport forms of the hormone. Here, we investigated the substrate preferences, oligomeric states, and structures of ADKs from moss (Physcomitrella patens) and maize (Zea mays) alongside metabolomic and phenotypic analyses. We showed that dexamethasone-inducible ZmADK overexpressor lines in Arabidopsis can benefit from a higher number of lateral roots and larger root areas under nitrogen starvation. We discovered that maize and moss enzymes can form dimers upon increasing protein concentration, setting them apart from the monomeric human and protozoal ADKs. Structural and kinetic analyses revealed a catalytically inactive unique dimer. Within the dimer, both active sites are mutually blocked. The activity of moss ADKs, exhibiting a higher propensity to dimerize, was 10-fold lower compared with maize ADKs. Two monomeric structures in a ternary complex highlight the characteristic transition from an open to a closed state upon substrate binding. This suggests that the oligomeric state switch can modulate the activity of moss ADKs and probably other plant ADKs. Moreover, dimer association represents a novel negative feedback mechanism, helping to maintain steady levels of adenosine and AMP.
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
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Experimental Botany
ISSN
0022-0957
e-ISSN
1460-2431
Volume of the periodical
76
Issue of the periodical within the volume
12
Country of publishing house
US - UNITED STATES
Number of pages
23
Pages from-to
3457-3479
UT code for WoS article
001474122700001
EID of the result in the Scopus database
2-s2.0-105013839482