Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic

Dang, Chi V.

doi:10.1042/bj2390249

Cited by 46 publications

(30 citation statements)

References 88 publications

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“…Although catalytic domains from homologous synthetases are highly conserved from bacteria to mammals, mammalian ARSs have acquired unique peptide appendices that are not present in the corresponding prokaryotic enzymes (1)(2)(3). Eight of the mammalian ARSs are found in a high molecular weight multi-ARS complex with three noncatalytic proteins, p43, p38, and p18, whereas the corresponding bacterial ARSs do not form such a complex (1)(2)(3)(4). This suggests that the peptide appendices might be involved in protein-protein interactions within the multi-ARS complex.…”

mentioning

confidence: 93%

Catalytic Peptide of Human Glutaminyl-tRNA Synthetase Is Essential for Its Assembly to the Aminoacyl-tRNA Synthetase Complex

Kim¹,

Park²,

Kim³

et al. 2000

Journal of Biological Chemistry

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Human glutaminyl-tRNA synthetase (QRS) is one of several mammalian aminoacyl-tRNA synthetases (ARSs) that form a macromolecular protein complex. To understand the mechanism of QRS targeting to the multi-ARS complex, we analyzed both exogenous and endogenous QRSs by immunoprecipitation after overexpression of various Myc-tagged QRS mutants in human embryonic kidney 293 cells. Whereas a deletion mutant containing only the catalytic domain (QRS-C) was targeted to the multi-ARS complex, a mutant QRS containing only the N-terminal appended domain (QRS-N) was not. Deletion mapping showed that the ATP-binding Rossman fold was necessary for targeting of QRS to the multi-ARS complex. Furthermore, exogenous Myc-tagged QRS-C was co-immunoprecipitated with endogenous QRS. Since glutaminylation of tRNA was dramatically increased in cells transfected with the full-length QRS, but not with either QRS-C or QRS-N, both the QRS catalytic domain and the N-terminal appended domain were required for full aminoacylation activity. When QRS-C was overexpressed, arginyl-tRNA synthetase and p43 were released from the multi-ARS complex along with endogenous QRS, suggesting that the N-terminal appendix of QRS is required to keep arginyl-tRNA synthetase and p43 within the complex. Thus, the eukaryote-specific N-terminal appendix of QRS appears to stabilize the association of other components in the multi-ARS complex, whereas the C-terminal catalytic domain is necessary for QRS association with the multi-ARS complex.Aminoacyl-tRNA synthetases (ARSs) 1 catalyze the ligation of a specific amino acid to its cognate tRNA, thereby ensuring the faithful translation of genetic code. Although catalytic domains from homologous synthetases are highly conserved from bacteria to mammals, mammalian ARSs have acquired unique peptide appendices that are not present in the corresponding prokaryotic enzymes (1-3). Eight of the mammalian ARSs are found in a high molecular weight multi-ARS complex with three noncatalytic proteins, p43, p38, and p18, whereas the corresponding bacterial ARSs do not form such a complex (1-4). This suggests that the peptide appendices might be involved in protein-protein interactions within the multi-ARS complex. Furthermore, intact rat aspartyl-tRNA synthetase (DRS) associates in vivo with the multi-ARS complex, whereas the Nterminal appendix-deleted form does not (5), indicating that the appended domain is indispensable for targeting DRS to this complex. Protein-protein interactions between the appendices of various ARSs have previously been shown using the yeast two-hybrid system (6). Similarly, p43 associates with the Nterminal appendix of human arginyl-tRNA synthetase (RRS), stimulating its aminoacylation activity (7).In addition to a role in protein-protein interactions, ARS appended domains could also enhance aminoacylation activity by recruiting tRNAs. Previously it has been shown that the N-terminal appended domain of yeast QRS nonspecifically binds to both double-and single-stranded RNA (8). Fusion of this domain to Esch...

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confidence: 93%

Catalytic Peptide of Human Glutaminyl-tRNA Synthetase Is Essential for Its Assembly to the Aminoacyl-tRNA Synthetase Complex

Kim¹,

Park²,

Kim³

et al. 2000

Journal of Biological Chemistry

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“…Despite the common catalytic role of these enzymes, cytoplasmic tRNA synthetases of higher eukaryotes differ from their lower eukaryotic or prokaryotic counterparts in forming a multiprotein complex (1)(2)(3)(4). These multiprotein complexes are known to contain nine synthetases, which react with Glu, Pro, Ile, Leu, Met, Lys, Gln, Arg, and Asp (5).…”

mentioning

confidence: 99%

“…In human glutamyl-prolyl-tRNA synthetase (EPRS), 1 two domains exhibiting each enzyme activity are connected by a linker that contains three tandemly repeated motifs of 57 amino acids (7). The human prolyl-tRNA synthetase lacking this linker peptide was still active, suggesting that it is not essential for catalytic activity (8).…”

mentioning

confidence: 99%

A Multifunctional Repeated Motif Is Present in Human Bifunctional tRNA Synthetase

Rho¹,

Lee²,

Jeong³

et al. 1998

Journal of Biological Chemistry

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Tandem repeats located in the human bifunctional glutamyl-prolyl-tRNA synthetase (EPRS) have been found in many different eukaryotic tRNA synthetases and were previously shown to interact with another distinct repeated motifs in human isoleucyl-tRNA synthetase. Nuclear magnetic resonance and differential scanning calorimetry analyses of an isolated EPRS repeat showed that it consists of a helix-turn-helix with a melting temperature of 59°C. Specific interaction of the EPRS repeats with those of isoleucyl-tRNA synthetase was confirmed by in vitro binding assays and shown to have a dissociation constant of approximately 2.9 M. The EPRS repeats also showed the binding activity to the N-terminal motif of arginyl-tRNA synthetase as well as to various nucleic acids, including tRNA. Results of the present work suggest that the region comprising the repeated motifs of EPRS provides potential sites for interactions with various biological molecules and thus plays diverse roles in the cell.

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“…The enzyme activity was assayed in the reaction of tRNA ~'' aminoacylation, SerRS from rabbit liver was purified by the same method [3].…”

Section: Purification Of Serrsmentioning

confidence: 99%

Immuno‐chemical non‐cross‐reactivity between eukaryotic and prokaryotic seryl‐tRNA synthetases

et al. 1991

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Monospecific polyclonal antibodies (pAbs) against highly purified bovine seryl-tRNA synthetase (SerRS, EC 6.1.1.1) were prepared and their specificity tested. The interactions of pAbs with SerRS from different organisms were investigated by protein immunoblotting and ELISA methods. pAbs inhibit eukaryotic SerRS aminoacylating activity and exert no effect on SerRS activity from prokaryotes. It is proposed that prokaryotic and eukaryotic SerRS evolve from different ancestor genes.Seryl-tRNA synthetase: Monospecific polyclonal antibody: Immunochemical cross-reaction

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Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic

Cited by 46 publications

References 88 publications

Catalytic Peptide of Human Glutaminyl-tRNA Synthetase Is Essential for Its Assembly to the Aminoacyl-tRNA Synthetase Complex

Catalytic Peptide of Human Glutaminyl-tRNA Synthetase Is Essential for Its Assembly to the Aminoacyl-tRNA Synthetase Complex

A Multifunctional Repeated Motif Is Present in Human Bifunctional tRNA Synthetase

Immuno‐chemical non‐cross‐reactivity between eukaryotic and prokaryotic seryl‐tRNA synthetases

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Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic

Cited by 46 publications

References 88 publications

Catalytic Peptide of Human Glutaminyl-tRNA Synthetase Is Essential for Its Assembly to the Aminoacyl-tRNA Synthetase Complex

Catalytic Peptide of Human Glutaminyl-tRNA Synthetase Is Essential for Its Assembly to the Aminoacyl-tRNA Synthetase Complex

A Multifunctional Repeated Motif Is Present in Human Bifunctional tRNA Synthetase

Immuno&#x2010;chemical non&#x2010;cross&#x2010;reactivity between eukaryotic and prokaryotic seryl&#x2010;tRNA synthetases

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Immuno‐chemical non‐cross‐reactivity between eukaryotic and prokaryotic seryl‐tRNA synthetases