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Pregled bibliografske jedinice broj: 982118

Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase


Kekez, Mario; Zanki, Vladimir; Kekez, Ivana; Baranašić, Jurica; Hodnik, Vesna; Duchêne, Anne- Marie; Anderluh, Gregor; Gruić Sovulj, Ita; Matković-Čalogović, Dubravka; Weygand-Đurašević, Ivana; Rokov Plavec, Jasmina
Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase // The FEBS journal, 286 (2019), 3; 536-554 doi:10.1111/febs.14735 (međunarodna recenzija, članak, znanstveni)


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Naslov
Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase

Autori
Kekez, Mario ; Zanki, Vladimir ; Kekez, Ivana ; Baranašić, Jurica ; Hodnik, Vesna ; Duchêne, Anne- Marie ; Anderluh, Gregor ; Gruić Sovulj, Ita ; Matković-Čalogović, Dubravka ; Weygand-Đurašević, Ivana ; Rokov Plavec, Jasmina

Izvornik
The FEBS journal (1742-464X) 286 (2019), 3; 536-554

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
aminoacyl-tRNA synthetase ; disulfide bond ; BEN1 ; protein-protein interaction ; brassinosteroid

Sažetak
The rules of the genetic code are established by aminoacyl-tRNA synthetases (aaRSs) enzymes, which covalently link tRNA with the cognate amino acid. Many aaRSs are involved in diverse cellular processes beyond translation, acting alone, or in complex with other proteins. However, studies of aaRS noncanonical assembly and functions in plants are scarce, as are structural studies of plant aaRSs. Here, we have solved the crystal structure of Arabidopsis thaliana cytosolic seryl-tRNA synthetase (SerRS), which is the first crystallographic structure of a plant aaRS. Arabidopsis SerRS displays structural features typical of canonical SerRSs, except for a unique intrasubunit disulfide bridge. In a yeast two- hybrid screen, we identified BEN1, a protein involved in the metabolism of plant brassinosteroid hormones, as a protein interactor of Arabidopsis SerRS. The SerRS:BEN1 complex is one of the first protein complexes of plant aaRSs discovered so far, and is a rare example of an aaRS interacting with an enzyme involved in primary or secondary metabolism. To pinpoint regions responsible for this interaction, we created truncated variants of SerRS and BEN1, and identified that the interaction interface involves the SerRS globular catalytic domain and the N-terminal extension of BEN1 protein. BEN1 does not have a strong impact on SerRS aminoacylation activity, indicating that the primary function of the complex is not the modification of SerRS canonical activity. Perhaps SerRS performs as yet unknown noncanonical functions mediated by BEN1. These findings indicate that – via SerRS and BEN1 – a link exists between the protein translation and steroid metabolic pathways of the plant cell.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija



POVEZANOST RADA


Projekti:
HRZZ-IP-2016-06-6272 - Aminoacil-tRNA-sintetaze kao čuvari standardnog genetičkog koda (AARSCODE) (Gruić Sovulj, Ita, HRZZ - 2016-06) ( POIROT)
HRZZ-IS-09.01/293 - Nekanonske uloge aminoacil-tRNA-sintetaza

Ustanove:
Prirodoslovno-matematički fakultet, Zagreb

Poveznice na cjeloviti tekst rada:

doi rdcu.be doi.org febs.onlinelibrary.wiley.com

Citiraj ovu publikaciju:

Kekez, Mario; Zanki, Vladimir; Kekez, Ivana; Baranašić, Jurica; Hodnik, Vesna; Duchêne, Anne- Marie; Anderluh, Gregor; Gruić Sovulj, Ita; Matković-Čalogović, Dubravka; Weygand-Đurašević, Ivana; Rokov Plavec, Jasmina
Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase // The FEBS journal, 286 (2019), 3; 536-554 doi:10.1111/febs.14735 (međunarodna recenzija, članak, znanstveni)
Kekez, M., Zanki, V., Kekez, I., Baranašić, J., Hodnik, V., Duchêne, A., Anderluh, G., Gruić Sovulj, I., Matković-Čalogović, D., Weygand-Đurašević, I. & Rokov Plavec, J. (2019) Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase. The FEBS journal, 286 (3), 536-554 doi:10.1111/febs.14735.
@article{article, author = {Kekez, Mario and Zanki, Vladimir and Kekez, Ivana and Barana\v{s}i\'{c}, Jurica and Hodnik, Vesna and Duch\^{e}ne, Anne- Marie and Anderluh, Gregor and Grui\'{c} Sovulj, Ita and Matkovi\'{c}-\v{C}alogovi\'{c}, Dubravka and Weygand-\DJura\v{s}evi\'{c}, Ivana and Rokov Plavec, Jasmina}, year = {2019}, pages = {536-554}, DOI = {10.1111/febs.14735}, keywords = {aminoacyl-tRNA synthetase, disulfide bond, BEN1, protein-protein interaction, brassinosteroid}, journal = {The FEBS journal}, doi = {10.1111/febs.14735}, volume = {286}, number = {3}, issn = {1742-464X}, title = {Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase}, keyword = {aminoacyl-tRNA synthetase, disulfide bond, BEN1, protein-protein interaction, brassinosteroid} }
@article{article, author = {Kekez, Mario and Zanki, Vladimir and Kekez, Ivana and Barana\v{s}i\'{c}, Jurica and Hodnik, Vesna and Duch\^{e}ne, Anne- Marie and Anderluh, Gregor and Grui\'{c} Sovulj, Ita and Matkovi\'{c}-\v{C}alogovi\'{c}, Dubravka and Weygand-\DJura\v{s}evi\'{c}, Ivana and Rokov Plavec, Jasmina}, year = {2019}, pages = {536-554}, DOI = {10.1111/febs.14735}, keywords = {aminoacyl-tRNA synthetase, disulfide bond, BEN1, protein-protein interaction, brassinosteroid}, journal = {The FEBS journal}, doi = {10.1111/febs.14735}, volume = {286}, number = {3}, issn = {1742-464X}, title = {Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase}, keyword = {aminoacyl-tRNA synthetase, disulfide bond, BEN1, protein-protein interaction, brassinosteroid} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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