Discrimination between transfer-RNAs by tyrosyl-tRNA synthetase

The ‘KMSKS' Motif in Tyrosyl-tRNA Synthetase Participates in the Initial Binding of tRNATyr

“…The ‘KFGKT' sequence continues to interact with adenosine 76 during formation of the E·[Tyr-tRNA Tyr ·AMP] ⧧ complex, although the strength of this interaction does not change during formation of this transition state complex. This mechanism is consistent with the model proposed by Bedouelle and colleagues ( − ) for the interaction of tyrosyl-tRNA synthetase with tRNA Tyr . In their model, the only nucleotide in tRNA Tyr that the ‘KFGKT' sequence is positioned to interact with is adenosine 76, and even this interaction requires that the ‘KFGKT' sequence moves 5−10 Å toward the active site of the enzyme.…”

The ‘KMSKS' Motif in Tyrosyl-tRNA Synthetase Participates in the Initial Binding of tRNATyr

“…The ‘KFGKT' sequence continues to interact with adenosine 76 during formation of the E·[Tyr-tRNA Tyr ·AMP] ⧧ complex, although the strength of this interaction does not change during formation of this transition state complex. This mechanism is consistent with the model proposed by Bedouelle and colleagues ( − ) for the interaction of tyrosyl-tRNA synthetase with tRNA Tyr . In their model, the only nucleotide in tRNA Tyr that the ‘KFGKT' sequence is positioned to interact with is adenosine 76, and even this interaction requires that the ‘KFGKT' sequence moves 5−10 Å toward the active site of the enzyme.…”

Peculiarities of aminoacyl-tRNA synthetases from trypanosomatids

“…Trypanosomatid MetRSs J o u r n a l P r e -p r o o f have at their N-terminus a glutathione Stransferase (GST)-like domain of ~210 aa (displaying 20% of sequence identity with the human GST and 25% with the GST-like domain appended to the human cytosolic MetRS, according to a SWISS-MODEL template search). Finally, it is known that TyrRS classically forms a homodimer and the binding-site for one molecule of tRNA Tyr straddles both subunits (32). In the case of trypanosomatids, our MSA confirms that TyrRS is a double-length enzyme that forms a pseudo-dimer, as previously observed for L. major and T. brucei TyrRSs (33,34).…”

Recognition of tRNAs with a long variable arm by aminoacyl-tRNA synthetases

“…The mode of binding tRNA to TyrRSTT is similar to the earlier model of the TyrRS-tRNA Tyr complex proposed by Bedouelle [61] on the basis of extensive mutational studies and very similar to one proposed by us on the basis of the study of phosphate protection upon tRNA Tyr binding to the synthetase [62]. Despite having an unambiguous class I catalytic domain, TyrRS in contrast to the canonical class I systems has a class II mode of tRNA recognition [60].…”

The ‘KMSKS' Motif in Tyrosyl-tRNA Synthetase Participates in the Initial Binding of tRNATyr

“…The ‘KFGKT' sequence continues to interact with adenosine 76 during formation of the E·[Tyr-tRNA Tyr ·AMP] ⧧ complex, although the strength of this interaction does not change during formation of this transition state complex. This mechanism is consistent with the model proposed by Bedouelle and colleagues ( − ) for the interaction of tyrosyl-tRNA synthetase with tRNA Tyr . In their model, the only nucleotide in tRNA Tyr that the ‘KFGKT' sequence is positioned to interact with is adenosine 76, and even this interaction requires that the ‘KFGKT' sequence moves 5−10 Å toward the active site of the enzyme.…”

Peculiarities of aminoacyl-tRNA synthetases from trypanosomatids

“…Trypanosomatid MetRSs J o u r n a l P r e -p r o o f have at their N-terminus a glutathione Stransferase (GST)-like domain of ~210 aa (displaying 20% of sequence identity with the human GST and 25% with the GST-like domain appended to the human cytosolic MetRS, according to a SWISS-MODEL template search). Finally, it is known that TyrRS classically forms a homodimer and the binding-site for one molecule of tRNA Tyr straddles both subunits (32). In the case of trypanosomatids, our MSA confirms that TyrRS is a double-length enzyme that forms a pseudo-dimer, as previously observed for L. major and T. brucei TyrRSs (33,34).…”

Recognition of tRNAs with a long variable arm by aminoacyl-tRNA synthetases

“…The mode of binding tRNA to TyrRSTT is similar to the earlier model of the TyrRS-tRNA Tyr complex proposed by Bedouelle [61] on the basis of extensive mutational studies and very similar to one proposed by us on the basis of the study of phosphate protection upon tRNA Tyr binding to the synthetase [62]. Despite having an unambiguous class I catalytic domain, TyrRS in contrast to the canonical class I systems has a class II mode of tRNA recognition [60].…”

The ‘KMSKS' Motif in Tyrosyl-tRNA Synthetase Participates in the Initial Binding of tRNATyr

“…The ‘KFGKT' sequence continues to interact with adenosine 76 during formation of the E·[Tyr-tRNA Tyr ·AMP] ⧧ complex, although the strength of this interaction does not change during formation of this transition state complex. This mechanism is consistent with the model proposed by Bedouelle and colleagues ( − ) for the interaction of tyrosyl-tRNA synthetase with tRNA Tyr . In their model, the only nucleotide in tRNA Tyr that the ‘KFGKT' sequence is positioned to interact with is adenosine 76, and even this interaction requires that the ‘KFGKT' sequence moves 5−10 Å toward the active site of the enzyme.…”

Peculiarities of aminoacyl-tRNA synthetases from trypanosomatids

“…Trypanosomatid MetRSs J o u r n a l P r e -p r o o f have at their N-terminus a glutathione Stransferase (GST)-like domain of ~210 aa (displaying 20% of sequence identity with the human GST and 25% with the GST-like domain appended to the human cytosolic MetRS, according to a SWISS-MODEL template search). Finally, it is known that TyrRS classically forms a homodimer and the binding-site for one molecule of tRNA Tyr straddles both subunits (32). In the case of trypanosomatids, our MSA confirms that TyrRS is a double-length enzyme that forms a pseudo-dimer, as previously observed for L. major and T. brucei TyrRSs (33,34).…”

Recognition of tRNAs with a long variable arm by aminoacyl-tRNA synthetases

“…The mode of binding tRNA to TyrRSTT is similar to the earlier model of the TyrRS-tRNA Tyr complex proposed by Bedouelle [61] on the basis of extensive mutational studies and very similar to one proposed by us on the basis of the study of phosphate protection upon tRNA Tyr binding to the synthetase [62]. Despite having an unambiguous class I catalytic domain, TyrRS in contrast to the canonical class I systems has a class II mode of tRNA recognition [60].…”