• Publications
  • Influence
Macromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly.
TLDR
Using an in vitro binding assay, concomitant association of several components of the complex on immobilized p38 could be demonstrated, and the involvement of synergistic effects for association of weakly interacting proteins was revealed. Expand
The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration.
TLDR
It is demonstrated that Parkin interacts with, ubiquitylates and promotes the degradation of p38, a key structural component of the mammalian aminoacyl-tRNA synthetase complex, opening the way for a detailed examination of its potential non-canonical role in neurodegeneration. Expand
Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein.
TLDR
It is suggested that p38, for which no homologous protein has been identified to date in organisms devoid of multisynthetase complexes, plays a pivotal role for the assembly of the subunits of the eukaryotic tRNA synthetase complex. Expand
The p43 Component of the Mammalian Multi-synthetase Complex Is Likely To Be the Precursor of the Endothelial Monocyte-activating Polypeptide II Cytokine*
TLDR
The results implicate the COOH-terminal moiety of p43 as a RNA binding domain in the native state, as a component of the multisynthetase complex, p43 may be required for tRNA channeling and, after proteolytic processing occurring in tumor cells, would acquire inflammatory properties possibly related to apoptosis. Expand
Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer.
TLDR
A molecular phylogenetic analysis was conducted on the 14 GlxRS (GluRS or GlnRS) sequences available to date, suggesting that bacterial Gln RS has a eukaryotic origin and was acquired by a mechanism of horizontal gene transfer. Expand
The N-terminal Domain of Mammalian Lysyl-tRNA Synthetase Is a Functional tRNA-binding Domain*
TLDR
These results provide new insights into tRNALys channeling in eukaryotic cells and shed new light on the possible requirement of native LysRS for triggering tRNA3 Lys packaging into human immunodeficiency virus, type 1 viral particles. Expand
Dissection of the Structural Organization of the Aminoacyl-tRNA Synthetase Complex*
TLDR
The assembly of the multiaminoacyl-tRNA synthetase complex (MARS) in human cells is examined, with data consistent with a structural role of the three nonsynthetase components of MARS, with p38 connecting two subcomplexes that may form in the absence of p38. Expand
Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A
TLDR
The data suggest that TCTP has guanine nucleotide dissociation inhibitor activity, and, moreover, implicate T CTP in the elongation step of protein synthesis. Expand
A recurrent RNA‐binding domain is appended to eukaryotic aminoacyl‐tRNA synthetases
TLDR
It is shown by gel retardation and filter binding experiments that the repeated units that build the linker region of the bifunctional glutamyl‐prolyl‐tRNA synthetase had a general RNA‐binding capacity. Expand
Modular evolution of the Glx-tRNA synthetase family--rooting of the evolutionary tree between the bacteria and archaea/eukarya branches.
TLDR
The analysis suggests that the ancestral GluRS-like enzyme was solely composed of the catalytic domain bearing the class-defining motifs of aminoacyl-tRNA synthetases, and that the anticodon-binding domain of GlxRSs was independently acquired in the bacteria and archaea branches of the universal tree of life. Expand
...
1
2
3
4
5
...