Histidyl-tRNAs and histidyl-tRNA synthetases in wild type and cytoplasmic petite mutants of Saccharomyces cerevisiae

Boguslawski, George; Vodkin, Michael H.; Finkelstein, David; Fink, Gerald R.

doi:10.1021/bi00719a030

Cited by 25 publications

(6 citation statements)

References 21 publications

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“…It is possible that some of the His-tRNA synthetase activity observed in liver was derived from mitochondria which, in some cases, contain aminoacyl-tRNA synthetases distinct from those in the cytosol. Heterogeneity of His-tRNA synthetase in yeast is attributable to distinct mitochondrial and cytosol enzymes (Boguslawski et al, 1974). Mitochondria are abundant in liver but scarce in reticulocytes (Bessis & Breton-Gorius, 1964), thus making the detection of a mitochondrial enzyme in the present study unlikely.…”

Section: Discussionmentioning

confidence: 74%

“…The enzyme acylates the two histidine tRNA isoacceptors of rabbit reticulocytes with similar Km values and at similar rates. typhimurium (DeLorenzo & Ames, 1970), Escherichia coli (Kalousek & Konigsberg, 1974), and Saccharomyces cerevesiae (Boguslawski et al, 1974), and the enzyme from each source has been partially characterized. Purification and characterization of this enzyme from animal cells have not, however, been reported previously.…”

mentioning

confidence: 99%

“…S. typhimurium. and baker's yeast (Kalousck & Konigsberg, 1974;DeLorenzo & Ames, 1970;Boguslawski et al, 1974). While a variety of subunit arrangements has been observed for different aminoacyl-tRNA synthetases, it has been noted (Muench et al, 1975) that the synthetases for any particular amino acid usually have the same subunit arrangement in a variety of organisms.…”

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confidence: 99%

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Purification and some properties of the histidyl-tRNA synthetase from the cytosol of rabbit reticulocytes

Kane¹,

Vugrincic²,

Finbloom³

et al. 1978

Biochemistry

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The histidyl-tRNA synthetase of rabbit reticulocyte cytosol has been purified 84 000-fold to apparent homogeneity with a specific activity of 687 nmol of histidyl-tRNA formed per min per mg of protein. Ten to 15% of the enzyme activity is sedimented with the ribosomes while the remainder is in the cytosol. The purified enzyme has a molecular weight of 122 000 as determined by sucrose density gradient centrifugation. Gel electrophoresis in the presence of 0.1% sodium dodecyl sulfate suggests that it is composed of two similar subunits with a molecular weight of approximately 64 000. The enzyme has a magnesium optimum of 45 mM; however, this is reduced to 5 mM in the presence of an intracellular potassium concentration (160 nM). The enzyme acylates the two histidine tRNA isoacceptors of rabbit reticulocytes with similar Km values and at similar rates.

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Section: Discussionmentioning

confidence: 74%

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confidence: 99%

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confidence: 99%

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Purification and some properties of the histidyl-tRNA synthetase from the cytosol of rabbit reticulocytes

Kane¹,

Vugrincic²,

Finbloom³

et al. 1978

Biochemistry

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“…The intracellular concentration of HisRS was estimated at 2.3 M in Salmonella E. coli Muench and Berg, 1966 820-fold 85 (42.5) Kalousek and Konigsberg, 1974 351-fold, Kern and Lapointe, partial 1979purification Fromant et al, 1981del Rio et al, 1982crystals Francklyn et al, 1994(HisRS Yan et al, 1996; mutants) Rühlmann et al, 1997;Francklyn, 1997 B. stearo-102 Grosjean et al, 1976 thermophilus S. typhimurium 800-fold, 100 De Lorenzo and Ames, 95% 1970 78 (40) De Lorenzo et al, 1972;Boguslawski et al,1974 T. thermophilus 95%, Yaremchuk et al, 1995 crystals Streptococcus 99% (47.9) Menguito et al, 1993a equisimilis Baker's yeast 590-fold Tigerstrom and Tener, 1967 S. cerevisiae 100 Boguslawski et al,1974 N. crassa Takeda, 1969 921-fold 125 (62.5) Chen and Somberg, 1980 Rat liver 100 -150 Yang et al, 1984 11700-96 (50) Fahoum and Yang,1987 fold multi-enzyme Badyopadhyay and complexes Deutscher, 1971Vellekamp et al, 1985Salomon et al, 1976multiOgata et al, 1994enzyme Ogata and Terea, 1994 Rabbit reti-83780-122 (64) Kane et al, 1978 culocytes fold partial Alzhanova et al, 1982purifiSmith et al, 1979 Beef liver partial Walker et al, 1983 purification Bovine liver Ͼ 2650-160 (80) Walker and Jeffrey, fold 1987 HeLa cells 5110-120 (55) Biswas et al, 1987a…”

Section: Purification Of Histidyl-trna Synthetasesmentioning

confidence: 99%

Histidyl-tRNA Synthetase

Freist¹,

Jf²,

Rühlmann³

et al. 1999

Biological Chemistry

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Histidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes.A compilation of currently known primary structures of HisRS shows that the subunits of these homodimeric enzymes consist of 420 -550 amino acid residues. This represents a relatively short chain length among aminoacyl-tRNA synthetases (aaRS), whose peptide chain sizes range from about 300 to 1100 amino acid residues.The crystal structures of HisRS from two organisms and their complexes with histidine, histidyl-adenylate and histidinol with ATP have been solved. HisRS from Escherichia coli and Thermus thermophilus are very similar dimeric enzymes consisting of three domains: the N-terminal catalytic domain containing the sixstranded antiparallel ␤-sheet and the three motifs characteristic of class II aaRS, a HisRS-specific helical domain inserted between motifs 2 and 3 that may contact the acceptor stem of the tRNA, and a C-terminal ␣/␤ domain that may be involved in the recognition of the anticodon stem and loop of tRNA His .The aminoacylation reaction follows the standard two-step mechanism. HisRS also belongs to the group of aaRS that can rapidly synthesize diadenosine tetraphosphate, a compound that is suspected to be involved in several regulatory mechanisms of cell metabolism. Many analogs of histidine have been tested for their properties as substrates or inhibitors of HisRS, leading to the elucidation of structure-activity relationships concerning configuration, importance of the carboxy and amino group, and the nature of the side chain.HisRS has been found to act as a particularly important antigen in autoimmune diseases such as rheumatic arthritis or myositis. Successful attempts have been made to identify epitopes responsible for the complexation with such auto-antibodies.

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“…Chloroplastic aminoacyl tRNA synthetases are nuclear coded (19) but very little is known about the coding origin of mit aminoacyl tRNA synthetases. Recently BOGUSLAWSKY et al (20) found a mit specific His-RS in a p0 mutant lacking mit DNA. This indicates that the mit enzyme is nuclear coded but the authors could not separate mit-and cyt His-RS by chromatography.…”

Section: Nucleic Acids Researchmentioning

confidence: 99%

Nuclear origin of specific yeast mitochondrial aminoacyl-tRNA synthetases

Schneller¹,

Schneller²,

Martin³

et al. 1976

Nucleic Acids Research

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Hydroxylapatite chromatographies of mitochondrial and total enzymes from a rho+ yeast, or from the related rho degrees mitochondrial DNA-less mutant, show the occurrence in the mitochondrial enzyme of one Phe-, one Met-, one Leu-tRNA synthetase peak which elutes distinctly from the cytoplasmic counterpart and charges well mitochondrial tRNA, whereas the cytoplasmic enzyme does not. The measurement of the mitochondrial synthetases activities in various enzymatic extracts shows that they are not repressed in rho+ cells grown on 10% glucose and that they are concentrated in the mitochondria (Phe- and Met- tRNA synthetases) but are also present outside the mitochondria. It is concluded that yeast mitochondrial protein biosynthesis involves the nuclear coded mitochondrial specific Phe-, Met- and Leu-tRNA synthetases and that the entrance of the synthetases into the mitochondria needs no factor depending on the mitochondrial DNA.

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Histidyl-tRNAs and histidyl-tRNA synthetases in wild type and cytoplasmic petite mutants of Saccharomyces cerevisiae

Cited by 25 publications

References 21 publications

Purification and some properties of the histidyl-tRNA synthetase from the cytosol of rabbit reticulocytes

Purification and some properties of the histidyl-tRNA synthetase from the cytosol of rabbit reticulocytes

Histidyl-tRNA Synthetase

Nuclear origin of specific yeast mitochondrial aminoacyl-tRNA synthetases

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