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OB or Not OB: Idiosyncratic utilization of the tRNA-binding OB-fold domain in unicellular, pathogenic eukaryotes.
Kapps, Delphine; Cela, Marta; Théobald-Dietrich, Anne; Hendrickson, Tamara; Frugier, Magali.
Afiliação
  • Kapps D; RNA Architecture and Reactivity, Strasbourg University, CNRS, IBMC, France.
  • Cela M; RNA Architecture and Reactivity, Strasbourg University, CNRS, IBMC, France.
  • Théobald-Dietrich A; RNA Architecture and Reactivity, Strasbourg University, CNRS, IBMC, France.
  • Hendrickson T; Department of Chemistry, Wayne State University, Detroit, MI, USA.
  • Frugier M; RNA Architecture and Reactivity, Strasbourg University, CNRS, IBMC, France.
FEBS Lett ; 590(23): 4180-4191, 2016 Dec.
Article em En | MEDLINE | ID: mdl-27714804
In this review, we examine the so-called OB-fold, a tRNA-binding domain homologous to the bacterial tRNA-binding protein Trbp111. We highlight the ability of OB-fold homologs to bind tRNA species and summarize their distribution in evolution. Nature has capitalized on the advantageous effects acquired when an OB-fold domain binds to tRNA by evolutionarily selecting this domain for fusion to different enzymes. Here, we review our current understanding of how the complexity of OB-fold-containing proteins and enzymes developed to expand their functions, especially in unicellular, pathogenic eukaryotes.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oligonucleotídeos / Oligossacarídeos / RNA de Transferência / Proteínas de Ligação a RNA / Eucariotos Limite: Animals / Humans Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oligonucleotídeos / Oligossacarídeos / RNA de Transferência / Proteínas de Ligação a RNA / Eucariotos Limite: Animals / Humans Idioma: En Ano de publicação: 2016 Tipo de documento: Article