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Arabidopsis seryl‐ tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl‐ tRNA synthetase
Author(s) -
Kekez Mario,
Zanki Vladimir,
Kekez Ivana,
Baranasic Jurica,
Hodnik Vesna,
Duchêne AnneMarie,
Anderluh Gregor,
GruicSovulj Ita,
MatkovićČalogović Dubravka,
WeygandDurasevic Ivana,
RokovPlavec Jasmina
Publication year - 2019
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14735
Subject(s) - aminoacylation , arabidopsis , biochemistry , transfer rna , aminoacyl trna synthetase , biology , saccharomyces cerevisiae , amino acid , arabidopsis thaliana , yeast , rna , mutant , gene
The rules of the genetic code are established by aminoacyl‐ tRNA synthetases (aa RS s) enzymes, which covalently link tRNA with the cognate amino acid. Many aa RS s are involved in diverse cellular processes beyond translation, acting alone, or in complex with other proteins. However, studies of aa RS noncanonical assembly and functions in plants are scarce, as are structural studies of plant aa RS s. Here, we have solved the crystal structure of Arabidopsis thaliana cytosolic seryl‐ tRNA synthetase (Ser RS ), which is the first crystallographic structure of a plant aa RS . Arabidopsis Ser RS displays structural features typical of canonical Ser RS s, except for a unique intrasubunit disulfide bridge. In a yeast two‐hybrid screen, we identified BEN 1, a protein involved in the metabolism of plant brassinosteroid hormones, as a protein interactor of Arabidopsis Ser RS . The Ser RS : BEN 1 complex is one of the first protein complexes of plant aa RS s discovered so far, and is a rare example of an aa RS interacting with an enzyme involved in primary or secondary metabolism. To pinpoint regions responsible for this interaction, we created truncated variants of Ser RS and BEN 1, and identified that the interaction interface involves the Ser RS globular catalytic domain and the N‐terminal extension of BEN 1 protein. BEN 1 does not have a strong impact on Ser RS aminoacylation activity, indicating that the primary function of the complex is not the modification of Ser RS canonical activity. Perhaps Ser RS performs as yet unknown noncanonical functions mediated by BEN 1. These findings indicate that – via Ser RS and BEN 1 – a link exists between the protein translation and steroid metabolic pathways of the plant cell. Database Structural data are available in the PDB under the accession number PDB ID 6GIR .