Seryl-tRNA synthetase specificity for tRNA(sec) in Bacterial Sec biosynthesis

Autor(es)

Fernandes, Adriano de Freitas ^[1] ; Serrao, Vitor Hugo Balasco ^{[1, 2]} ; Scortecci, Jessica Fernandes ^{[1, 3]} ; Thiemann, Otavio Henrique ^{[1, 4]}

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Phys Inst Sao Carlos, Trabalhador Sao Carlense Av 400, BR-13566590 Sao Carlos, SP - Brazil

^[2] Univ Toronto, Lab Med & Pathobiol, 1 Kings Coll Circle, Toronto, ON M5S 1A8 - Canada

^[3] Univ British Columbia, Dept Biochem & Mol Biol, 2350 Hlth Sci Mall, Vancouver, BC V6T 1Z3 - Canada

^[4] Fed Univ Sao Carlos UFSCar, Dept Genet & Evolut, BR-13565905 Sao Carlos 16, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS; v. 1868, n. 8 AUG 2020.
• Citações Web of Science: 0

Resumo

tRNA synthetases are responsible for decoding the molecular information, from codons to amino acids. Seryl-tRNA synthetase (SerRS), besides the five isoacceptors of tRNA(Ser), recognizes tRNAE({[}Ser]Sec) for the incorporation of selenocysteine (Sec, U) into selenoproteins. The selenocysteine synthesis pathway is known and is dependent on several protein-protein and protein-RNA interactions. Those interactions are not fully described, in particular, involving tRNA({[}Ser]Sec) and SerRS. Here we describe the molecular interactions between the Escherichia coli Seryl-tRNA synthetase (EcSerRS) and tRNA({[}Ser]Sec) Eserisee in order to determine their specificity, selectivity and binding order, leading to tRNA aminoacylation. The dissociation constant of EcSerRS and tRNA({[}Ser]Sec) was determined as (126 +/- 20) nM. We also demonstrate that EcSerRS binds initially to tRNAE({[}Ser]Sec) in the presence of ATP for further recognition by E. coli selenocysteine synthetase (EcSelA) for Ser to Sec conversion. The proposed studies clarify the mechanism of tRNAE({[}Ser]Sec) incorporation in Bacteria as well as of other domains of life. (AU)

• Processo FAPESP: 16/20977-7 - Estudo da via de incorporação de selenocisteínas: compreensão dos mecanismos de interações macromoleculares
• Beneficiário: Jessica Fernandes Scortecci
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 12/23730-1 - Caracterização das interações macromoleculares das proteínas envolvidas na síntese de selenocisteínas em escherichia coli
• Beneficiário: Vitor Hugo Balasco Serrão
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 14/16005-4 - Caracterização das interações moleculares entre proteínas da via de síntese de selenocisteínas
• Beneficiário: Jessica Fernandes Scortecci
• Modalidade de apoio: Bolsas no Brasil - Iniciação Científica