A monomer-dimer switch modulates the activity of plant
adenosine kinase

J 2025

A monomer-dimer switch modulates the activity of plant adenosine kinase

KOPECNY, David Jaroslav; Armelle VIGOUROUX; Jakub BELICEK; Martina KOPECNA; Radka KONCITIKOVA et al.

Základní údaje

Originální název

A monomer-dimer switch modulates the activity of plant adenosine kinase

Autoři

Vydání

Journal of Experimental Botany, OXFORD, Oxford University Press, 2025, 0022-0957

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10403 Physical chemistry

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 5.700 v roce 2024

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90242/25:00143938

Organizační jednotka

CIISB III

Klíčová slova anglicky

Adenosine kinase; crystal structure; cytokinin; overexpression; Physcomitrella patens; purine; riboside; SnRK; Zea mays

Štítky

CF BIC, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 11. 3. 2026 11:30, Mgr. Eva Dubská

Anotace

V originále

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.

Návaznosti

90242, velká výzkumná infrastruktura

Název: CIISB III

Citovat

KOPECNY, David Jaroslav; Armelle VIGOUROUX; Jakub BELICEK; Martina KOPECNA; Radka KONCITIKOVA; Jaroslava FRIEDECKA; Vaclav MIK; Klara SUPIKOVA; Jan Frantisek HUMPLIK; Le Berre MARINE; Stephan PLANCQUEEL; Miroslav STRNAD; von Schwartzenberg KLAUS; Ondrej NOVAK; Solange MORERA a David KOPECNY. A monomer-dimer switch modulates the activity of plant adenosine kinase. Journal of Experimental Botany. OXFORD: Oxford University Press, 2025, roč. 76, č. 12, s. 3457-3479. ISSN 0022-0957. Dostupné z: https://doi.org/10.1093/jxb/eraf094.

@article{2559701,
   author = {Kopecny, David Jaroslav and Vigouroux, Armelle and Belicek, Jakub and Kopecna, Martina and Koncitikova, Radka and Friedecka, Jaroslava and Mik, Vaclav and Supikova, Klara and Humplik, Jan Frantisek and Marine, Le Berre and Plancqueel, Stephan and Strnad, Miroslav and Klaus, von Schwartzenberg and Novak, Ondrej and Morera, Solange and Kopecny, David},
   article_location = {OXFORD},
   article_number = {12},
   doi = {https://doi.org/10.1093/jxb/eraf094},
   keywords = {Adenosine kinase; crystal structure; cytokinin; overexpression; Physcomitrella patens; purine; riboside; SnRK; Zea mays},
   language = {eng},
   issn = {0022-0957},
   journal = {Journal of Experimental Botany},
   title = {A monomer-dimer switch modulates the activity of plant adenosine kinase},
   url = {https://watermark02.silverchair.com/eraf094.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAA1gwggNUBgkqhkiG9w0BBwagggNFMIIDQQIBADCCAzoGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQMUcRMhTVGt6RpYhM_AgEQgIIDC_E_yGB4KHF4YpgesmObRPn_V6zBgWtFnKS1ttil2aMD},
   volume = {76},
   year = {2025}
}

TY  - JOUR
ID  - 2559701
AU  - Kopecny, David Jaroslav - Vigouroux, Armelle - Belicek, Jakub - Kopecna, Martina - Koncitikova, Radka - Friedecka, Jaroslava - Mik, Vaclav - Supikova, Klara - Humplik, Jan Frantisek - Marine, Le Berre - Plancqueel, Stephan - Strnad, Miroslav - Klaus, von Schwartzenberg - Novak, Ondrej - Morera, Solange - Kopecny, David
PY  - 2025
TI  - A monomer-dimer switch modulates the activity of plant adenosine kinase
JF  - Journal of Experimental Botany
VL  - 76
IS  - 12
SP  - 3457-3479
EP  - 3457-3479
PB  - Oxford University Press
SN  - 00220957
KW  - Adenosine kinase
KW  - crystal structure
KW  - cytokinin
KW  - overexpression
KW  - Physcomitrella patens
KW  - purine
KW  - riboside
KW  - SnRK
KW  - Zea mays
UR  - https://watermark02.silverchair.com/eraf094.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAA1gwggNUBgkqhkiG9w0BBwagggNFMIIDQQIBADCCAzoGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQMUcRMhTVGt6RpYhM_AgEQgIIDC_E_yGB4KHF4YpgesmObRPn_V6zBgWtFnKS1ttil2aMD
N2  - 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.
ER  -

KOPECNY, David Jaroslav; Armelle VIGOUROUX; Jakub BELICEK; Martina KOPECNA; Radka KONCITIKOVA; Jaroslava FRIEDECKA; Vaclav MIK; Klara SUPIKOVA; Jan Frantisek HUMPLIK; Le Berre MARINE; Stephan PLANCQUEEL; Miroslav STRNAD; von Schwartzenberg KLAUS; Ondrej NOVAK; Solange MORERA a David KOPECNY. A monomer-dimer switch modulates the activity of plant adenosine kinase. \textit{Journal of Experimental Botany}. OXFORD: Oxford University Press, 2025, roč.~76, č.~12, s.~3457-3479. ISSN~0022-0957. Dostupné z: https://doi.org/10.1093/jxb/eraf094.

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