Seryl-tRNA synthetase specificity for tRNASec in Bacterial Sec biosynthesis.
Biochim Biophys Acta Proteins Proteom
; 1868(8): 140438, 2020 08.
Article
en En
| MEDLINE
| ID: mdl-32330624
ABSTRACT
tRNA synthetases are responsible for decoding the molecular information, from codons to amino acids. Seryl-tRNA synthetase (SerRS), besides the five isoacceptors of tRNASer, recognizes tRNA[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 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 tRNA[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 tRNA[Ser]Sec incorporation in Bacteria as well as of other domains of life.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Asunto principal:
Serina-ARNt Ligasa
/
Transferasas
/
ARN de Transferencia Aminoácido-Específico
/
ARN de Transferencia de Cisteína
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Regulación Bacteriana de la Expresión Génica
/
Escherichia coli
Idioma:
En
Revista:
Biochim Biophys Acta Proteins Proteom
Año:
2020
Tipo del documento:
Article
País de afiliación:
Brasil