Chromosomal localization of human gene for histidyl-tRNA synthetase: Clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5

1986 ◽  
Vol 12 (5) ◽  
pp. 513-517 ◽  
Author(s):  
John J. Wasmuth ◽  
Leon R. Carlock
Keyword(s):  
Human Chromosome ◽  
Chromosomal Localization ◽  
Human Gene ◽  
Trna Synthetase ◽  
Chromosome 5 ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Genes Encoding ◽  
Human Chromosome 5

Genes encoding adrenergic receptors are not clustered on the long arm of human chromosome 5

1994 ◽  
Vol 67 (2) ◽  
pp. 69-74 ◽  
Author(s):  
S.K. Loftus ◽  
R. Shiang ◽  
J.A. Warrington ◽  
U. Bengtsson ◽  
J.D. McPherson ◽  
...  
Keyword(s):  
Human Chromosome ◽  
Adrenergic Receptors ◽  
Chromosome 5 ◽  
Genes Encoding ◽  
Human Chromosome 5

Selective linkage disruption in human-Chinese hamster cell hybrids: deletion mapping of the leuS, hexB, emtB, and chr genes on human chromosome 5

1982 ◽  
Vol 2 (10) ◽  
pp. 1220-1228
Author(s):  
S Dana ◽  
J J Wasmuth
Keyword(s):  
Human Chromosome ◽  
Mammalian Species ◽  
Chinese Hamster ◽  
Trna Synthetase ◽  
Gene Organization ◽  
Deletion Mapping ◽  
Chromosome 2 ◽  
Chromosome 5 ◽  
Human Chromosome 5 ◽  
Chinese Hamster Chromosome

Chinese hamster-human interspecific hybrid cells, which contain human chromosome 5 and express four genes linked on that chromosome, were subjected to selective conditions requiring them to retain one of the four linked genes, leuS (encoding leucyl-tRNA synthetase), but lose another, either emtB (encoding ribosomal protein S14) or chr. Cytogenetic and biochemical analyses of spontaneous segregants isolated by using these unique selective pressures have enabled us to determine the order and regional location of the leuS, hexB, emtB, and chr genes on human chromosome 5. These segregants arise primarily by terminal deletions of various portions of the long arm of chromosome 5. Our results indicate that the order of at least three of these genes is the same on human chromosome 5 and Chinese hamster chromosome 2. Thus, there appears to be extensive homology between Chinese hamster chromosome 2 and human chromosome 5, which represents an extreme example of the conservation of gene organization between very divergent mammalian species. In addition, these hybrids and selective conditions provide a very simple and quantitative means to assess the potency of various agents suspected of inducing gross chromosomal damage.

scholarly journals Selective linkage disruption in human-Chinese hamster cell hybrids: deletion mapping of the leuS, hexB, emtB, and chr genes on human chromosome 5.

1982 ◽  
Vol 2 (10) ◽  
pp. 1220-1228 ◽  
Author(s):  
S Dana ◽  
J J Wasmuth
Keyword(s):  
Human Chromosome ◽  
Mammalian Species ◽  
Chinese Hamster ◽  
Trna Synthetase ◽  
Gene Organization ◽  
Deletion Mapping ◽  
Chromosome 2 ◽  
Chromosome 5 ◽  
Human Chromosome 5 ◽  
Chinese Hamster Chromosome

Chinese hamster-human interspecific hybrid cells, which contain human chromosome 5 and express four genes linked on that chromosome, were subjected to selective conditions requiring them to retain one of the four linked genes, leuS (encoding leucyl-tRNA synthetase), but lose another, either emtB (encoding ribosomal protein S14) or chr. Cytogenetic and biochemical analyses of spontaneous segregants isolated by using these unique selective pressures have enabled us to determine the order and regional location of the leuS, hexB, emtB, and chr genes on human chromosome 5. These segregants arise primarily by terminal deletions of various portions of the long arm of chromosome 5. Our results indicate that the order of at least three of these genes is the same on human chromosome 5 and Chinese hamster chromosome 2. Thus, there appears to be extensive homology between Chinese hamster chromosome 2 and human chromosome 5, which represents an extreme example of the conservation of gene organization between very divergent mammalian species. In addition, these hybrids and selective conditions provide a very simple and quantitative means to assess the potency of various agents suspected of inducing gross chromosomal damage.

Chromosomal localization of the gene encoding GTPase-activating protein (RASA) to human chromosome 5, bands q13–q15

Genomics ◽  
1990 ◽  
Vol 6 (2) ◽  
pp. 383-385 ◽  
Author(s):  
Richard S. Lemons ◽  
Rafael Espinosa ◽  
Matt Rebentisch ◽  
Frank McCormick ◽  
Martha Ladner ◽  
...  
Keyword(s):  
Human Chromosome ◽  
Chromosomal Localization ◽  
Gtpase Activating Protein ◽  
Chromosome 5 ◽  
Gene Encoding ◽  
Human Chromosome 5

Threonyl-tRNA synthetase gene maps close to leucyl-tRNA synthetase gene on human chromosome 5

1986 ◽  
Vol 12 (5) ◽  
pp. 519-522 ◽  
Author(s):  
Steven C. Gerken ◽  
John J. Wasmuth ◽  
Stuart M. Arfin
Keyword(s):  
Human Chromosome ◽  
Trna Synthetase ◽  
Chromosome 5 ◽  
Gene Maps ◽  
Human Chromosome 5

scholarly journals Mitochondrial Aminoacyl-tRNA Synthetase and Disease: The Yeast Contribution for Functional Analysis of Novel Variants

2021 ◽  
Vol 22 (9) ◽  
pp. 4524
Author(s):  
Sonia Figuccia ◽  
Andrea Degiorgi ◽  
Camilla Ceccatelli Berti ◽  
Enrico Baruffini ◽  
Cristina Dallabona ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Trna Synthetase ◽  
Nuclear Genes ◽  
Model Systems ◽  
Causative Role ◽  
Mitochondrial Translation ◽  
Trna Synthetases ◽  
Mtdna Mutations ◽  
Aminoacyl Trna Synthetases ◽  
Genes Encoding

In most eukaryotes, mitochondrial protein synthesis is essential for oxidative phosphorylation (OXPHOS) as some subunits of the respiratory chain complexes are encoded by the mitochondrial DNA (mtDNA). Mutations affecting the mitochondrial translation apparatus have been identified as a major cause of mitochondrial diseases. These mutations include either heteroplasmic mtDNA mutations in genes encoding for the mitochondrial rRNA (mtrRNA) and tRNAs (mttRNAs) or mutations in nuclear genes encoding ribosomal proteins, initiation, elongation and termination factors, tRNA-modifying enzymes, and aminoacyl-tRNA synthetases (mtARSs). Aminoacyl-tRNA synthetases (ARSs) catalyze the attachment of specific amino acids to their cognate tRNAs. Differently from most mttRNAs, which are encoded by mitochondrial genome, mtARSs are encoded by nuclear genes and then imported into the mitochondria after translation in the cytosol. Due to the extensive use of next-generation sequencing (NGS), an increasing number of mtARSs variants associated with large clinical heterogeneity have been identified in recent years. Being most of these variants private or sporadic, it is crucial to assess their causative role in the disease by functional analysis in model systems. This review will focus on the contributions of the yeast Saccharomyces cerevisiae in the functional validation of mutations found in mtARSs genes associated with human disorders.

scholarly journals Inhibitory mechanism of reveromycin A at the tRNA binding site of a class I synthetase

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Bingyi Chen ◽  
Siting Luo ◽  
Songxuan Zhang ◽  
Yingchen Ju ◽  
Qiong Gu ◽  
...  
Keyword(s):  
Binding Site ◽  
Catalytic Domain ◽  
Trna Synthetase ◽  
Rational Drug Design ◽  
Class I ◽  
Binding Assays ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Rational Drug ◽  
Trna Binding

AbstractThe polyketide natural product reveromycin A (RM-A) exhibits antifungal, anticancer, anti-bone metastasis, anti-periodontitis and anti-osteoporosis activities by selectively inhibiting eukaryotic cytoplasmic isoleucyl-tRNA synthetase (IleRS). Herein, a co-crystal structure suggests that the RM-A molecule occupies the substrate tRNAIle binding site of Saccharomyces cerevisiae IleRS (ScIleRS), by partially mimicking the binding of tRNAIle. RM-A binding is facilitated by the copurified intermediate product isoleucyl-adenylate (Ile-AMP). The binding assays confirm that RM-A competes with tRNAIle while binding synergistically with l-isoleucine or intermediate analogue Ile-AMS to the aminoacylation pocket of ScIleRS. This study highlights that the vast tRNA binding site of the Rossmann-fold catalytic domain of class I aminoacyl-tRNA synthetases could be targeted by a small molecule. This finding will inform future rational drug design.

scholarly journals Lysyl-tRNA synthetase from Escherichia coli K12. Chromatographic heterogeneity and the lysU-gene product

1987 ◽  
Vol 248 (1) ◽  
pp. 43-51 ◽  
Author(s):  
J Charlier ◽  
R Sanchez
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
Activity Ratio ◽  
Deae Cellulose ◽  
Trna Synthetase ◽  
Trna Synthetases ◽  
E Coli ◽  
Aminoacyl Trna Synthetases

In contrast with most aminoacyl-tRNA synthetases, the lysyl-tRNA synthetase of Escherichia coli is coded for by two genes, the normal lysS gene and the inducible lysU gene. During its purification from E. coli K12, lysyl-tRNA synthetase was monitored by its aminoacylation and adenosine(5′)tetraphospho(5′)adenosine (Ap4A) synthesis activities. Ap4A synthesis was measured by a new assay using DEAE-cellulose filters. The heterogeneity of lysyl-tRNA synthetase (LysRS) was revealed on hydroxyapatite; we focused on the first peak, LysRS1, because of its higher Ap4A/lysyl-tRNA activity ratio at that stage. Additional differences between LysRS1 and LysRS2 (major peak on hydroxyapatite) were collected. LysRS1 was eluted from phosphocellulose in the presence of the substrates, whereas LysRS2 was not. Phosphocellulose chromatography was used to show the increase of LysRS1 in cells submitted to heat shock. Also, the Mg2+ optimum in the Ap4A-synthesis reaction is much higher for LysRS1. LysRS1 showed a higher thermostability, which was specifically enhanced by Zn2+. These results in vivo and in vitro strongly suggest that LysRS1 is the heat-inducible lysU-gene product.

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