Share This Author
The Last Piece in the Vitamin B1 Biosynthesis Puzzle
- Sandrine Coquille, C. Roux, T. Fitzpatrick, S. Thore
- Biology, ChemistryThe Journal of Biological Chemistry
- 9 October 2012
Mutational and yeast complementation studies identify the key residues for HMP-P biosynthesis as well as the use of pyridoxal 5′-phosphate as a substrate rather than as a cofactor, and could show that iron binding to H MP-P synthase is essential for the reaction.
An artificial PPR scaffold for programmable RNA recognition.
The atomic structures of these artificial PPR domains elucidate the structural basis for their stability and modelling of RNA-protein interactions provides mechanistic insights into the importance ofRNA-binding residues and suggests modes of PPR-RNA association.
High-resolution crystal structure of the eukaryotic HMP-P synthase (THIC) from Arabidopsis thaliana.
Redescription of Testudotaenia testudo (Magath, 1924) (Eucestoda: Proteocephalidea), a parasite of Apalone spinifera (Le Sueur) (Reptilia: Trionychidae) and Amia calva L. (Pisces: Amiidae) in North…
Testudotaenia testudo (Magath, 1924) is redescribed from the intestine of the softshell turtle Apalone spinifera (Le Sueur) (Trionychidae) and the bowfin Amia calva Linnaeus (Amiidae) from Reelfoot…
Polyuridylation in Eukaryotes: A 3′-End Modification Regulating RNA Life
- Paola Munoz-Tello, L. Rajappa, Sandrine Coquille, S. Thore
- BiologyBioMed research international
- 11 May 2015
The present review aims at summarizing the current knowledge on the various processes leading to RNA 3′-end uridylation and on their potential impacts in various diseases.
Crystal structure of HMP synthase Thi5 from S. cerevisiae
Crystal structure of eukaryotic THIC from A. thaliana
Crystal structure of designed cPPR-NRE protein
Leigh Syndrome-inducing Mutations Affect LRPPRC / SLIRP Complex Formation
This work demonstrates that SLIRP interacts with the N-terminal region of LRPPRC in a RNA independent manner and shows that the complex is stable in presence of high salt concentration.