The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors

Fett, Radegunde; Knippers, Rolf

doi:10.1016/s0021-9258(18)52315-2

Cited by 79 publications

(7 citation statements)

References 38 publications

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“…Sequence Analyses. Previous genetic and biochemical studies have identified the genes for ProRSs from E. coli (1), D. melanogaster (23), and H. sapiens (19,24). Although the sequence identity between fly and human ProRSs is high (58%), the similarities between E. coli and fly or E. coli and human are very low (20 and 19%, respectively) compared to those of some other aminoacyl-tRNA synthetases [for instance, the sequence similarity between human and E. coli alanyl-tRNA synthetases (AlaRSs) is 41% (34)].…”

Section: Resultsmentioning

confidence: 99%

“…Multiple sequence alignments were performed using the PILEUP program provided by the Genetics Computer Group (Madison, WI). Sequences used for alignments were obtained from published ProRS sequences [E. coli (1), Zymomonas mobilis (22), Drosophila melanogaster (23), and Homo sapiens (24)], from genome databases [Haemophilus influenzae (25), Mycoplasma genitalium (26), Mycoplasma pneumoniae (27), Synechocystis sp. PCC6803 (28), Methanococcus jannaschii (29), S. cereVisiae (cytoplasmic and mitochondrial) (a web site of the Saccharomyces Genome Database), Neisseria gonorrhoeae and Streptococcus pyogenes (a web site of the University of Oklahoma's Advanced Center for Genome Technology, April 26, 1997, data release), Methanobacterium thermoautotrophicum (30), Helicobacter pylori (31), and Archaeoglobus fulgidus (32)], and from similarity searches in the Genbank database [Chlamydia trachomatis (L25105), Mycobacterium tuberculosis (Z95207), Candida albican (U86341), and Caenorhabditis elegans (U00037)].…”

Section: Methodsmentioning

confidence: 99%

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Species-Specific Differences in the Operational RNA Code for Aminoacylation of tRNA^Pro

et al. 1998

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An operational RNA code relates amino acids to specific structural features located in tRNA acceptor stems. In contrast to the universal nature of the genetic code, the operational RNA code can vary in evolution due to coadaptations of the contacts between aminoacyl-tRNA synthetases and the acceptor stems of their cognate tRNA substrates. Here we demonstrate that, for class II prolyl-tRNA synthetase (ProRS), functional coadaptations have occurred in going from the bacterial to the human enzyme. Analysis of 20 ProRS sequences that cover all three taxonomic domains (bacteria, eucarya, and archaea) revealed that the sequences are divided into two evolutionarily distant groups. Aminoacylation assays showed that, while anticodon recognition has been maintained through evolution, significant changes in acceptor stem recognition have occurred. Whereas all tRNAPro sequences from bacteria strictly conserve A73 and C1.G72, all available cytoplasmic eukaryotic tRNAPro sequences have a C73 and a G1.C72 base pair. In contrast to the Escherichia coli synthetase, the human enzyme does not use these elements as major recognition determinants, since mutations at these positions have only small effects on cognate synthetase charging. Additionally, E. coli tRNAPro is a poor substrate for human ProRS, and the presence of the human anticodon-D stem biloop domain was necessary and sufficient to confer efficient aminoacylation by human ProRS on a chimeric tRNAPro containing the E. coli acceptor-TpsiC stem-loop domain. Our data suggest that the two ProRS groups may reflect coadaptations needed to accommodate changes in the operational RNA code for proline.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Species-Specific Differences in the Operational RNA Code for Aminoacylation of tRNA^Pro

et al. 1998

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“…In this instance, the extra domain is appended to the N-terminus and is similar to a domain found in eukaryote tRNA synthetases for histidine, glycine, and methionine (35)(36)(37). It is also repeated as three tandem domains that join human glutamyl-with prolyl-tRNA synthetase to give the Glu-Pro tRNA synthetase that is found in higher eukaryotes (38). As isolated domains, the peptides have helix-turn-helix structures that bind tRNA (39,40).…”

Section: Translation Proteins and Cell Signaling: A New Paradigm Emap...mentioning

confidence: 99%

Activation of Angiogenic Signaling Pathways by Two Human tRNA Synthetases

Ewalt

Schimmel

2002

Biochemistry

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Aminoacyl-tRNA synthetases establish the rules of the genetic code by joining amino acids to tRNAs that bear the anticodon triplets corresponding to the attached amino acids. The enzymes are thought to be among the earliest proteins to appear, in the transition from a putative RNA world to the theater of proteins. Over their long evolution, the enzymes have acquired additional functions that typically require specialized insertions or domain fusions. Recently, fragments of the closely related human tyrosyl- and tryptophanyl-tRNA synthetases were discovered to be active in angiogenesis signaling pathways. One synthetase fragment has proangiogenic activity, while the other is antiangiogenic. Activity was demonstrated in cell-based assays in vitro and in vivo in the chick embryo, and in the neonatal and adult mouse. The full-length, native enzymes are inactive in these same assays. Activation of angiogenesis activity requires fragment production from the native enzymes by protease cleavage or by translation of alternatively spliced pre-mRNA. Thus, these tRNA synthetases link translation to a major cell-signaling pathway in mammalian cells. The results with animals suggest that therapeutic applications are possible with these tRNA synthetases.

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“…The proteins eluted from the column were resolved by gel electrophoresis. MRS and two other complex-components, EPRS (Fett and Knippers, 1991) and p43 (Quevillon et al, 1997), were detected by immunoblotting with their respective antibodies. The majority of the three proteins were coeluted in the void volume as expected.…”

Section: Nucleolar Localization Of Mrsmentioning

confidence: 99%

Nucleolar Localization of Human Methionyl–Trna Synthetase and Its Role in Ribosomal RNA Synthesis

Ko¹,

Kang²,

Kim³

et al. 2000

The Journal of Cell Biology

109

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Human aminoacyl–tRNA synthetases (ARSs) are normally located in cytoplasm and are involved in protein synthesis. In the present work, we found that human methionyl–tRNA synthetase (MRS) was translocated to nucleolus in proliferative cells, but disappeared in quiescent cells. The nucleolar localization of MRS was triggered by various growth factors such as insulin, PDGF, and EGF. The presence of MRS in nucleoli depended on the integrity of RNA and the activity of RNA polymerase I in the nucleolus. The ribosomal RNA synthesis was specifically decreased by the treatment of anti-MRS antibody as determined by nuclear run-on assay and immunostaining with anti-Br antibody after incorporating Br-UTP into nascent RNA. Thus, human MRS plays a role in the biogenesis of rRNA in nucleoli, while it is catalytically involved in protein synthesis in cytoplasm.

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The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors

Cited by 79 publications

References 38 publications

Species-Specific Differences in the Operational RNA Code for Aminoacylation of tRNA^Pro

Species-Specific Differences in the Operational RNA Code for Aminoacylation of tRNA^Pro

Activation of Angiogenic Signaling Pathways by Two Human tRNA Synthetases

Nucleolar Localization of Human Methionyl–Trna Synthetase and Its Role in Ribosomal RNA Synthesis

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The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors

Cited by 79 publications

References 38 publications

Species-Specific Differences in the Operational RNA Code for Aminoacylation of tRNAPro

Species-Specific Differences in the Operational RNA Code for Aminoacylation of tRNAPro

Activation of Angiogenic Signaling Pathways by Two Human tRNA Synthetases

Nucleolar Localization of Human Methionyl–Trna Synthetase and Its Role in Ribosomal RNA Synthesis

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Product

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Species-Specific Differences in the Operational RNA Code for Aminoacylation of tRNA^Pro

Species-Specific Differences in the Operational RNA Code for Aminoacylation of tRNA^Pro