Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 3 de 3
Filtrar
Mais filtros











Intervalo de ano de publicação
1.
Biochemistry ; 60(6): 477-488, 2021 02 16.
Artigo em Inglês | MEDLINE | ID: mdl-33523633

RESUMO

Aminoacylated tRNAs are the substrates for ribosomal protein synthesis in all branches of life, implying an ancient origin for aminoacylation chemistry. In the 1970s, Orgel and colleagues reported potentially prebiotic routes to aminoacylated nucleotides and their RNA-templated condensation to form amino acid-bridged dinucleotides. However, it is unclear whether such reactions would have aided or impeded non-enzymatic RNA replication. Determining whether aminoacylated RNAs could have been advantageous in evolution prior to the emergence of protein synthesis remains a key challenge. We therefore tested the ability of aminoacylated RNA to participate in both templated primer extension and ligation reactions. We find that at low magnesium concentrations that favor fatty acid-based protocells, these reactions proceed orders of magnitude more rapidly than when initiated from the cis-diol of unmodified RNA. We further demonstrate that amino acid-bridged RNAs can act as templates in a subsequent round of copying. Our results suggest that aminoacylation facilitated non-enzymatic RNA replication, thus outlining a potentially primordial functional link between aminoacylation chemistry and RNA replication.


Assuntos
Aminoacilação de RNA de Transferência/fisiologia , Aminoacilação/fisiologia , Fosfatos de Dinucleosídeos/metabolismo , Conformação de Ácido Nucleico , Nucleotídeos/metabolismo , RNA/metabolismo , Moldes Genéticos , Aminoacilação de RNA de Transferência/genética
2.
FEBS Lett ; 587(20): 3360-4, 2013 Oct 11.
Artigo em Inglês | MEDLINE | ID: mdl-24021645

RESUMO

Class I and II aminoacyl-tRNA synthetases (AARSs) attach amino acids to the 2'- and 3'-OH of the tRNA terminal adenosine, respectively. One exception is phenylalanyl-tRNA synthetase (PheRS), which belongs to Class II but attaches phenylalanine to the 2'-OH. Here we show that two Class II AARSs, O-phosphoseryl- (SepRS) and pyrrolysyl-tRNA (PylRS) synthetases, aminoacylate the 2'- and 3'-OH, respectively. Structure-based-phylogenetic analysis reveals that SepRS is more closely related to PheRS than PylRS, suggesting that the idiosyncratic feature of 2'-OH acylation evolved after the split between PheRS and PylRS. Our work completes the understanding of tRNA aminoacylation positions for the 22 natural AARSs.


Assuntos
Aminoacil-tRNA Sintetases/metabolismo , Fenilalanina-tRNA Ligase/metabolismo , Aminoácidos/metabolismo , Aminoacil-tRNA Sintetases/química , Aminoacil-tRNA Sintetases/classificação , Aminoacil-tRNA Sintetases/genética , Aminoacilação/genética , Aminoacilação/fisiologia , Fenilalanina-tRNA Ligase/química , Fenilalanina-tRNA Ligase/classificação , Fenilalanina-tRNA Ligase/genética , Filogenia
3.
Rev. invest. clín ; 44(3): 427-39, jul.-sept. 1992. tab
Artigo em Inglês | LILACS | ID: lil-118284

RESUMO

En esta revisión se describen los diferentes sistemas de transporte para aminoácidos, la caracterización de éstos y de sus componentes, los factores que afectan las características cinéticas de los acarreadores específicos de los sistemas de transporte, y la importancia del transporte de aminoácidos en el mantenimiento de las concentraciones plasmáticas e intracelulares de aminoácidos en diversos tejidos, así como su papel en el control del metabolismo de aminoácidos.


Assuntos
Aminoacil-tRNA Sintetases/fisiologia , Aminoácidos/metabolismo , Aminoacilação/fisiologia
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA