Literature DB >> 27714804

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

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.
© 2016 Federation of European Biochemical Societies.

Keywords:  Trbp111; parasites; pathogenic eukaryotes; tRNA-binding protein

Mesh:

Substances:

Year:  2016        PMID: 27714804     DOI: 10.1002/1873-3468.12441

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Bioinformatic Analysis Reveals Archaeal tRNATyr and tRNATrp Identities in Bacteria.

Authors:  Takahito Mukai; Noah M Reynolds; Ana Crnković; Dieter Söll
Journal:  Life (Basel)       Date:  2017-02-21

2.  Identification of host tRNAs preferentially recognized by the Plasmodium surface protein tRip.

Authors:  Marta Cela; Anne Théobald-Dietrich; Joëlle Rudinger-Thirion; Philippe Wolff; Renaud Geslain; Magali Frugier
Journal:  Nucleic Acids Res       Date:  2021-10-11       Impact factor: 16.971

3.  Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein.

Authors:  José R Jaramillo Ponce; Delphine Kapps; Caroline Paulus; Johana Chicher; Magali Frugier
Journal:  J Biol Chem       Date:  2022-04-27       Impact factor: 5.486

  3 in total

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