Daniel Kern

Yeast mitochondrial Gln-tRNAGln is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS (2009)

Frechin, Mathieu, Senger, Bruno, Brayé, Mélanie, Kern, Daniel, Martin, Robert Pierre, Becker, Hubert Dominique

It is impossible to predict which pathway, direct glutaminylation of tRNAGln or tRNA-dependent transamidation of glutamyl-tRNAGln, generates mitochondrial glutaminyl-tRNAGln for protein synthesis in...

Bank of America (2008)

Remco Chang, Mohammad Ghoniem, Robert Kosara, William Ribarsky, Jing Yang, Evan Suma, ...

Large financial institutions such as Bank of America handle hundreds of thousands of wire transactions per day. Although most transactions are legitimate, these institutions have legal and financial...

EU - DIALOG & KOMMUNIKATION (2008)

Kern, Daniel, Rasmussen, Laurits

From next school year governmental regulations require more focus on the EU in primary school curriculum. At technical schools and other educational establishments within trade and business they have...

Structural elements defining elongation factor Tu mediated suppression of codon ambiguity (2007)

Roy, Hervé, Becker, Hubert Dominique, Mazauric, Marie-Hélène, Kern, Daniel

In most prokaryotes Asn-tRNAAsn and Gln-tRNAGln are formed by amidation of aspartate and glutamate mischarged onto tRNAAsn and tRNAGln, respectively. Coexistence in the organism of mischarged...

Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation (2007)

Deniziak, Marzanna, Sauter, Claude, Becker, Hubert Dominique, Paulus, Caroline Alexandra, Giegé, Richard, Kern, Daniel

Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein...

Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation (2007)

Deniziak, Marzanna, Sauter, Claude, Becker, Hubert Dominique, Paulus, Caroline Alexandra, Giegé, Richard, Kern, Daniel

Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein...

A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine (2006)

Bailly, Marc, Giannouli, Stamatina, Blaise, Mickael, Stathopoulos, Constantinos, Kern, Daniel, Becker, Hubert Dominique

In many prokaryotes and in organelles asparagine and glutamine are formed by a tRNA-dependent amidotransferase (AdT) that catalyzes amidation of aspartate and glutamate, respectively, mischarged on...

A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine (2006)

Bailly, Marc, Giannouli, Stamatina, Blaise, Mickael, Stathopoulos, Constantinos, Kern, Daniel, Becker, Hubert Dominique

In many prokaryotes and in organelles asparagine and glutamine are formed by a tRNA-dependent amidotransferase (AdT) that catalyzes amidation of aspartate and glutamate, respectively, mischarged on...

A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine (2006)

Bailly, Marc, Giannouli, Stamatina, Blaise, Mickael, Stathopoulos, Constantinos, Kern, Daniel, Becker, Hubert Dominique

In many prokaryotes and in organelles asparagine and glutamine are formed by a tRNA-dependent amidotransferase (AdT) that catalyzes amidation of aspartate and glutamate, respectively, mischarged on...

A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon (2004)

Blaise, Mickaël, Becker, Hubert Dominique, Keith, Gérard, Cambillau, Christian, Lapointe, Jacques, Giegé, Richard, ...

Escherichia coli encodes YadB, a protein displaying 34% identity with the catalytic core of glutamyl‐tRNA synthetase but lacking the anticodon‐binding domain. We show that YadB is a...

Volatile Decision Dynamics: Experiments, Stochastic Description, Intermittency Control, and Traffic Optimization (2001)

Helbing, Dirk, Schoenhof, Martin, Kern, Daniel

The coordinated and efficient distribution of limited resources by individual decisions is a fundamental, unsolved problem. When individuals compete for road capacities, time, space, money, goods,...

Footprinting of tRNAPhe transcripts from Thermus thermophilus HB8 with the homologues phenylalanyl-tRNA synthetase reveals a novel mode of interaction (1995)

Kreutzer, Roland, Kern, Daniel, Giegè, R., Rudinger, Joëlle

The phosphates of the tRNAPhe transcript from Thermus thermophilus interacting with the cognate synthetase were determined by footprinting. Backbone bond protection against cleavage by iodine of the...

The glutamyl-tRNA synthetase of Escherichia coil: substrate-induced protection against its thermal inactivation (1979)

Kern, Daniel, Lapointe, Jacques

The substrates-induced protection against the heat-inactivation of the glutamyl-tRNA synthetase has been investigated. tRNAG°u and ATP protect efficiently the enzyme, whereas glutamate does not. In...

Thermus thermophilus: A link in evolution of the tRNA-dependent amino acid amidation pathways

Becker, Hubert Dominique, Kern, Daniel

Thermus thermophilus possesses an aspartyl-tRNA synthetase (AspRS2) able to aspartylate efficiently tRNAAsp and tRNAAsn. Aspartate mischarged on tRNAAsn then is converted into asparagine by an ω...

Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain

Charron, Christophe, Roy, Hervé, Blaise, Mickael, Giegé, Richard, Kern, Daniel

In most organisms, tRNA aminoacylation is ensured by 20 aminoacyl-tRNA synthetases (aaRSs). In eubacteria, however, synthetases can be duplicated as in Thermus thermophilus, which contains two...

When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism

Roy, Hervé, Becker, Hubert Dominique, Reinbolt, Joseph, Kern, Daniel

Faithful protein synthesis relies on a family of essential enzymes called aminoacyl-tRNA synthetases, assembled in a piecewise fashion. Analysis of the completed archaeal genomes reveals that all...

A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon

Blaise, Mickaël, Becker, Hubert Dominique, Keith, Gérard, Cambillau, Christian, Lapointe, Jacques, Giegé, Richard, ...

Escherichia coli encodes YadB, a protein displaying 34% identity with the catalytic core of glutamyl-tRNA synthetase but lacking the anticodon-binding domain. We show that YadB is a tRNA modifying...

An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp

Dubois, Daniel Y., Blaise, Mickaël, Becker, Hubert D., Campanacci, Valérie, Keith, Gérard, Giegé, Richard, ...

The product of the Escherichia coli yadB gene is homologous to the N-terminal part of bacterial glutamyl-tRNA synthetases (GluRSs), including the Rossmann fold with the acceptor-binding domain and...

Thermus thermophilus: A link in evolution of the tRNA-dependent amino acid amidation pathways

Becker, Hubert Dominique, Kern, Daniel

Thermus thermophilus possesses an aspartyl-tRNA synthetase (AspRS2) able to aspartylate efficiently tRNAAsp and tRNAAsn. Aspartate mischarged on tRNAAsn then is converted into asparagine by an ω...

Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain

Charron, Christophe, Roy, Hervé, Blaise, Mickael, Giegé, Richard, Kern, Daniel

In most organisms, tRNA aminoacylation is ensured by 20 aminoacyl-tRNA synthetases (aaRSs). In eubacteria, however, synthetases can be duplicated as in Thermus thermophilus, which contains two...

When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism

Roy, Hervé, Becker, Hubert Dominique, Reinbolt, Joseph, Kern, Daniel

Faithful protein synthesis relies on a family of essential enzymes called aminoacyl-tRNA synthetases, assembled in a piecewise fashion. Analysis of the completed archaeal genomes reveals that all...

A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon

Blaise, Mickaël, Becker, Hubert Dominique, Keith, Gérard, Cambillau, Christian, Lapointe, Jacques, Giegé, Richard, ...

Escherichia coli encodes YadB, a protein displaying 34% identity with the catalytic core of glutamyl-tRNA synthetase but lacking the anticodon-binding domain. We show that YadB is a tRNA modifying...

An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp

Dubois, Daniel Y., Blaise, Mickaël, Becker, Hubert D., Campanacci, Valérie, Keith, Gérard, Giegé, Richard, ...

The product of the Escherichia coli yadB gene is homologous to the N-terminal part of bacterial glutamyl-tRNA synthetases (GluRSs), including the Rossmann fold with the acceptor-binding domain and...

A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine

Bailly, Marc, Giannouli, Stamatina, Blaise, Mickael, Stathopoulos, Constantinos, Kern, Daniel, Becker, Hubert Dominique

In many prokaryotes and in organelles asparagine and glutamine are formed by a tRNA-dependent amidotransferase (AdT) that catalyzes amidation of aspartate and glutamate, respectively, mischarged on...

Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation

Deniziak, Marzanna, Sauter, Claude, Becker, Hubert Dominique, Paulus, Caroline Alexandra, Giegé, Richard, Kern, Daniel

Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein...

Structural elements defining elongation factor Tu mediated suppression of codon ambiguity

Roy, Hervé, Becker, Hubert Dominique, Mazauric, Marie-Hélène, Kern, Daniel

In most prokaryotes Asn-tRNAAsn and Gln-tRNAGln are formed by amidation of aspartate and glutamate mischarged onto tRNAAsn and tRNAGln, respectively. Coexistence in the organism of mischarged...

Dual-targeted tRNA-dependent amidotransferase ensures both mitochondrial and chloroplastic Gln-tRNAGln synthesis in plants

Pujol, Claire, Bailly, Marc, Kern, Daniel, Maréchal-Drouard, Laurence, Becker, Hubert, Duchêne, Anne-Marie

Aminoacyl-tRNAs are generally formed by direct attachment of an amino acid to tRNAs by aminoacyl-tRNA synthetases, but Gln-tRNA is an exception to this rule. Gln-tRNAGln is formed by this direct...

Yeast mitochondrial Gln-tRNAGln is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS

Frechin, Mathieu, Senger, Bruno, Brayé, Mélanie, Kern, Daniel, Martin, Robert Pierre, Becker, Hubert Dominique

It is impossible to predict which pathway, direct glutaminylation of tRNAGln or tRNA-dependent transamidation of glutamyl-tRNAGln, generates mitochondrial glutaminyl-tRNAGln for protein synthesis in...