Premium
OB or Not OB: Idiosyncratic utilization of the tRNA‐binding OB‐fold domain in unicellular, pathogenic eukaryotes
Author(s) -
Kapps Delphine,
Cela Marta,
ThéobaldDietrich Anne,
Hendrickson Tamara,
Frugier Magali
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12441
Subject(s) - transfer rna , homologous chromosome , biology , binding domain , enzyme , microbiology and biotechnology , genetics , computational biology , biochemistry , binding site , rna , gene
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.