| Full text | |
| Author(s): |
Fernandes, Adriano de Freitas
[1]
;
Serrao, Vitor Hugo Balasco
[1, 2]
;
Scortecci, Jessica Fernandes
[1, 3]
;
Thiemann, Otavio Henrique
[1, 4]
Total Authors: 4
|
| Affiliation: | [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
Total Affiliations: 4
|
| Document type: | Journal article |
| Source: | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS; v. 1868, n. 8 AUG 2020. |
| Web of Science Citations: | 0 |
| Abstract | |
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) | |
| FAPESP's process: | 16/20977-7 - Study of the selenocysteine incorporation pathway: understanding the macromolecular interaction mechanism |
| Grantee: | Jessica Fernandes Scortecci |
| Support Opportunities: | Scholarships in Brazil - Doctorate (Direct) |
| FAPESP's process: | 12/23730-1 - Characterization of macromolecular interactions of proteins involved in the selenocysteine synthesis from Escherichia coli |
| Grantee: | Vitor Hugo Balasco Serrão |
| Support Opportunities: | Scholarships in Brazil - Doctorate |
| FAPESP's process: | 14/16005-4 - Characterization of the molecular interactions within selenocysteine synthesis pathway proteins |
| Grantee: | Jessica Fernandes Scortecci |
| Support Opportunities: | Scholarships in Brazil - Scientific Initiation |