M3i

@article{,

title = {OB or Not OB: Idiosyncratic utilization of the tRNA-binding OB-fold domain in unicellular, pathogenic eukaryotes.},

author = {D Kapps and M Cela and A Théobald-Dietrich and T Hendrickson and M Frugier},

url = {https://www.ncbi.nlm.nih.gov/pubmed/27714804?dopt=Abstract},

doi = {10.1002/1873-3468.12441},

isbn = {27714804},

year  = {2016},

date = {2016-01-01},

journal = {FEBS Lett},

volume = {590},

number = {23},

pages = {4180-4191},

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 tRNAs 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. This article is protected by copyright. All rights reserved.},

keywords = {FRUGIER, Trbp111 parasites pathogenic eukaryotes tRNA binding protein, Unité ARN},

pubstate = {published},

tppubtype = {article}

}