Fractionation of yeast mitochondrial tRNA<sup>Tyr</sup> and tRNA<sup>Leu</sup>

Schneller, Jean-Marie; Accoceberry, B.; Stahl, A

doi:10.1016/0014-5793(75)80678-8

Cited by 12 publications

(3 citation statements)

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“…Isolation of in vivo 32P-labeled mitochondrial tRNA has been reported previously (Martin, R. P., et al, 1977). Preparation procedures of total-cell and mitochondrial aminoacyl-tRNA ligases (crude extracts) and tRNA aminoacylation have been described elsewhere (Accoceberry et al, 1973;Schneller et al, 1975bSchneller et al, , 1976. Cytoplasmic tRNA was acylated by total-cell enzyme or postmitochondrial enzyme at pH 7.4 and mitochondrial tRNA was acylated by mitochondrial enzyme at pH 8 by using [14C]lysine (sp act.…”

Section: Lysis Of Mitochondria Preparation Of Submitochondrialmentioning

confidence: 99%

Import of nuclear deoxyribonucleic acid coded lysine-accepting transfer ribonucleic acid (anticodon C-U-U) into yeast mitochondria

Martin¹,

Schneller²,

Stahl³

et al. 1979

Biochemistry

140

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Section: Lysis Of Mitochondria Preparation Of Submitochondrialmentioning

confidence: 99%

Import of nuclear deoxyribonucleic acid coded lysine-accepting transfer ribonucleic acid (anticodon C-U-U) into yeast mitochondria

Martin¹,

Schneller²,

Stahl³

et al. 1979

Biochemistry

140

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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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“…No subclass III GRPs were identified in Curcuma longa EST data bank. Absence of subclass III GRPs has also been reported in other monocotyledonous plants [25]. However, Fusaro et al [15] has reportedly isolated ten RNA binding GRPs of subclass III in the sugarcane EST data bank.…”

Section: Resultsmentioning

confidence: 99%

Classification and comparative analysis of Curcuma longa L. expressed sequences tags (ESTs) encoding glycine-rich proteins (GRPs)

Kar¹,

Nayak²,

Joshi³

2012

Bioinformation

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Glycine-rich proteins (GRPs) are a group of proteins characterized by their high content of glycine residues often occurring in repetitive blocs. The diverse expression pattern and sub cellular localization of various GRPs suggest their implication in different physiological processes. Several GRPs has been isolated and characterized from different monocots and dicots. However, little or no information is available about the structure and function of GRPs in asexually reproducing plants. In this study, in-silico analysis of expressed sequence tag database resulted in the isolation of fifty-one GRPs from Curcuma longa L., an asexually reproducible plant of great medicinal and economic significance. Phylogenetic analysis grouped the GRPs into four distinct classes based on conserved motifs and nature of glycine-rich repeats. Majority of the isolated GRPs exhibited high homology with known GRPs from other plants that are expressed in response to various stresses. The presence of high structural diversity and signal peptide in some GRPs suggest their diverse physiological role and tissue specific localization. The isolated sequences can be used as a framework for cloning, characterization and expressional analysis of GRPs in response to various biotic and abiotic stresses in Curcuma longa as well as other asexually reproducing plants.

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Fractionation of yeast mitochondrial tRNA^Tyr and tRNA^Leu

Cited by 12 publications

References 10 publications

Import of nuclear deoxyribonucleic acid coded lysine-accepting transfer ribonucleic acid (anticodon C-U-U) into yeast mitochondria

Import of nuclear deoxyribonucleic acid coded lysine-accepting transfer ribonucleic acid (anticodon C-U-U) into yeast mitochondria

Nuclear origin of specific yeast mitochondrial aminoacyl-tRNA synthetases

Classification and comparative analysis of Curcuma longa L. expressed sequences tags (ESTs) encoding glycine-rich proteins (GRPs)

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Fractionation of yeast mitochondrial tRNATyr and tRNALeu

Cited by 12 publications

References 10 publications

Import of nuclear deoxyribonucleic acid coded lysine-accepting transfer ribonucleic acid (anticodon C-U-U) into yeast mitochondria

Import of nuclear deoxyribonucleic acid coded lysine-accepting transfer ribonucleic acid (anticodon C-U-U) into yeast mitochondria

Nuclear origin of specific yeast mitochondrial aminoacyl-tRNA synthetases

Classification and comparative analysis of Curcuma longa L. expressed sequences tags (ESTs) encoding glycine-rich proteins (GRPs)

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Fractionation of yeast mitochondrial tRNA^Tyr and tRNA^Leu