Studies of odd bases in yeast mitochondrial tRNA: Absence of the fluorescent “Y” base in mitochondrial DNA coded tRNAPhe, absence of 4-thiouridine

Schneller, Jean-Marie; Martin, Robert P.; Stahl, A; Dirheimer, G.

doi:10.1016/0006-291x(75)90153-9

Cited by 17 publications

(4 citation statements)

References 16 publications

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“…Mitochondria isolation procedure from yeast protoplasts was the same as in (6) and mit. tRNA preparation was described in (7). E32P]-mit.…”

Section: Information Retrieval Limited I Falconberg Court London Wlmentioning

confidence: 99%

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Study of yeast mitochondrial tRNAs by two-dimensional polyacrylamide gel electrophoresis: characterization of isoaccepting species and search for imported cytoplasmic tRNAs

Martin¹,

Schneller²,

Stahl³

et al. 1977

Nucl Acids Res

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By two-dimensional polyacrylamide gel electrophoresis, yeast mitochondrial tRNA is fractionated into 27 major species. All but 6 of them migrate distinctly from cytoplasmic tRNAs. Migration of mitochondrial DNA-coded mitochondrial tRNAs shows the occurence of only one cytoplasmic tRNA in mitochondria. Several mitochondrial tRNA spots are identified on the electrophoregrams, some of them show isoaccepting species (Val, Ser, Met, Leu). It is suggested that there are sufficient mitochondrial tRNA genes on yeast mitochondrial DNA to allow mitochondrial protein biosynthesis by the mitochondrial tRNAs alone. Guanosine + Cytidine content and rate base composition are reported for some individual species. Mitochondrial tRNAPhe lacks Ribothymidine.

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“…Mitochondria isolation procedure from yeast protoplasts was the same as in (6) and mit. tRNA preparation was described in (7). E32P]-mit.…”

Section: Information Retrieval Limited I Falconberg Court London Wlmentioning

confidence: 99%

“…We suggest, as earlier pointed out for some individual mit. tRNA species (7,23), that the mit. DNAcoded mit.…”

Section: Metmentioning

confidence: 99%

Study of yeast mitochondrial tRNAs by two-dimensional polyacrylamide gel electrophoresis: characterization of isoaccepting species and search for imported cytoplasmic tRNAs

Martin¹,

Schneller²,

Stahl³

et al. 1977

Nucl Acids Res

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“…We reported the existence in the yeast Saccharomyces cerevisiae of mit tRNA species with a chromatographic behaviour different from that of their cytoplasmic counterparts (1,2,3,6). Hybridization experiments on unfractionated (4) or fractionated (5, 6) mit tRNA species showed that they are coded by mit DNA.…”

Section: Introductionmentioning

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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“…We therefore estimate that this step improves the purification procedure by removal of small-molecular-mass proteases and nucleases. mitochondria and extraction of mt-tRNA were as described in [23]. Total mitochondrial tRNA (Azao = 500) was fractionated on a 0.9 x 180-cm RPC5 column in 10 mM sodium acetate pH 4.5, 10 mM MgC12, 2 mM 2-mercaptoethanol eluted with the same buffer with a linear gradient (2 x 1 1) of 0.35-0.75 M NaCI.…”

Section: Purification Of Mitochondrial Methionyl-trna Synthetasementioning

confidence: 99%

Purification of the yeast mitochondrial methionyl‐tRNA synthetase

Schwob

Sanni

Fasiolo

et al. 1988

European Journal of Biochemistry

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Yeast-mitochondria1 methionyl-tRNA synthetase was purified 1060-fold from mitochondrial matrix proteins of Saccharomyces cerevisiae using a four-step procedure based on affinity chromatography (heparin-Ultrogel, tRNAMe'-Sepharose, Agarose-hexyl-AMP) to yield a single polypeptide of high specific activity (1800 U/mg). Like the cytoplasmic methionyl-tRNA synthetase ( M , 85 000), the mitochondrial isoenzyme is a monomer, but of significantly smaller polypeptide size ( M , 65 000). In contrast, the corresponding enzyme of Escherichia coli is a dimer (Mr 152000) made up of identical subunits. The measured affinity constants of the purified mitochondrial enzyme for methionine and tRNA'" are similar to those of the cytoplasmic isoenzyme. However, the two yeast enzymes exhibit clearly different patterns of aminoacylation of heterologous yeast and E. coli tRNAMe'. Furthermore, polyclonal antibodies raised against the two proteins did not show any cross-reactivity by inhibition of enzymatic activity and by the highly sensitive immunoblotting technique, indicating that the two enzymes share little, if any, common antigenic determinants. Taken together, our results further support the belief that the yeast mitochondrial and cytoplasmic methionyl-tRNA synthetases are different proteins coded for by two distinct nuclear genes.Like the yeast cytoplasmic aminoacyl-tRNA synthetases, the mitochondrial enzymes displayed affinity for immobilized heparin. This distinguishes them from the corresponding enzymes of E. coli. Such an unexpected property of the mitochondrial enzymes suggests that they have acquired during evolution a domain for binding to negatively charged cellular components.The components of the yeast mitochondrial translation apparatus are of dual origin. While the mitochondrial (mt) DNA codes for a complete set of transfer RNAs and the 15s and 21s ribosomal RNAs, the proteins required for mitochondrial protein synthesis such as the ribosomal proteins, the aminoacyl-tRNA synthetases, and the translation factors are coded for by nuclear genes. The sole exception is the ribosomal protein varl which is encoded by the mt DNA (for reviews, see [l, 21).Aminoacyl-tRNA synthetases constitute a divergent family of enzymes differing in size and subunit structure but catalyzing the same reaction, the selective attachment of amino acids to their cognate tRNAs. The molecular and catalytic properties of these enzymes have been extensively studied over the past 20 years [3, 41. However, information about mitochondrial aminoacyl-t RNA synthetases remained scarce until recently. Previous studies on phenylalanyl-, leucyl-, and methionyl-tRNA synthetases from yeast mitochondria and cytoplasm indicated that the two isoenzymes exhibit distinctive properties [5 -71. By contrast, no significant differences could be observed between the mitochondrial and cytoplasmic valyl-tRNA synthetases IS]. Recently, cloning and molecular analysis of genes coding for mitochondrial aminoacyl-tRNA synthetases revealed the existence of two classes of nuclea...

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Studies of odd bases in yeast mitochondrial tRNA: Absence of the fluorescent “Y” base in mitochondrial DNA coded tRNAPhe, absence of 4-thiouridine

Cited by 17 publications

References 16 publications

Study of yeast mitochondrial tRNAs by two-dimensional polyacrylamide gel electrophoresis: characterization of isoaccepting species and search for imported cytoplasmic tRNAs

Study of yeast mitochondrial tRNAs by two-dimensional polyacrylamide gel electrophoresis: characterization of isoaccepting species and search for imported cytoplasmic tRNAs

Nuclear origin of specific yeast mitochondrial aminoacyl-tRNA synthetases

Purification of the yeast mitochondrial methionyl‐tRNA synthetase

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