| Literature DB >> 27714804 |
Delphine Kapps1, Marta Cela1, Anne Théobald-Dietrich1, Tamara Hendrickson2, Magali Frugier1.
Abstract
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.Keywords: Trbp111; parasites; pathogenic eukaryotes; tRNA-binding protein
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Year: 2016 PMID: 27714804 DOI: 10.1002/1873-3468.12441
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124