Yeast ribosomal proteins

Otaka, Eiko; Kobata, Kenji

doi:10.1007/bf00268851

Cited by 50 publications

(34 citation statements)

References 35 publications

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“…We assumed that the basic amino acids were labelled by methyl group transfer. The neutral amino acid were extracted from sucrose-gradient-purified subunits and submitted to two-dimensional polyacrylamide gel electrophoresis according to [12]. After staining with Coomassic blue.…”

Section: Results a N D Discussionmentioning

confidence: 99%

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Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae

et al. 1984

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The occurrence of methylated proteins in the ribosomes of Saccharomyces cerevisiue was investigated by tracing the transfer of radioactive methyl groups from S-adenosyl methionine, taken up by growing cells, into the protein moiety of ribosomes. It was estimated that the large subunit contained about 10 protein-bound methyl groups distributed mainly among proteins YL23, YL32 and YL1. The small subunit contained at most 2 -4 methyl groups in proteins. Methyl groups could be transferred in vifro to proteins YL23 and YL32 in extracts from cultures of an Sadenosyl methionine auxotroph deprived of the methyl-group donor. In the most heavily methylated proteins the methylated amino acids formed in vitro were the same as those found in vivo (monomethyllysine and dimethyllysine in YL32; dimethyl and trimethyllysine in YL23). It is concluded that the enzymatic reaction in vitro faithfully saturates with methyl groups the target amino acids which are normally fully methylated in zjiz>o.

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Section: Results a N D Discussionmentioning

confidence: 99%

“…The two-dimensional electrophoresis was as described by Otaka and Kobata [12]. The 3H-labelled proteins wcre detected by lluorography on Kodak X-Omat AR films.…”

Section: Gel Electrophoresismentioning

confidence: 99%

Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae

et al. 1984

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“…Proteins from 60 S subunits of Saccharomyces cerevisiae ribosomes were isolated as in [9]. Protein 44 was purified by CM-cellulose column chromatography in the presence of 6 M urea and 0.5 mM DTT with a linear gradient from 0.05-0.65 M sodium acetate buffer (pH 5.5) followed by Sephadex G-100 gel filtration.…”

Section: Methodsmentioning

confidence: 99%

The primary structure of protein 44 from the large subunit of yeast ribosomes

Itoh¹,

Wittmann-Liebold²

1978

FEBS Letters

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“…Some ribosomal proteins have been reported to be sensitive to oxidation [13,14] or to be affected by protease(s) [15]. The 40s and 60s ribosomes from unfertilized and fertilized eggs of P .…”

Section: Protein L31mentioning

confidence: 99%

“…No alteration of electrophoretic profiles could be detected in the egg-specific and embryo-specific proteins, nor for the other protein components (results not shown). In the three species, the proteins prepared from the KCI-washed 80s ribosomes, the puromycin/KCl-washed 80s ribosomes and the 40s and 60s subunits were oxidized with performic acid [13]. Some of the proteins occupied different electrophoretic positions or appeared as two electrophoretically distinct forms.…”

Section: Protein L31mentioning

confidence: 99%

Modification of ribosomal proteins in sea urchin eggs following fertilization

Takeshima¹,

Nakano²

1983

European Journal of Biochemistry

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Analysis of the ribosomal proteins in sea urchin eggs by two-dimensional polyacrylamide gel electrophoresis revealed postfertilization changes in the proteins of both the small and the large subunits. Five egg-ribosomal proteins (S7, S16, S19, L19, L31) appeared to undergo rapid changes to the corresponding embryo-specific proteins. These changes were completed within 30 min after fertilization, and identical electrophoretic patterns were observed among the different developmental stages of embryos. One of the five proteins, S7, showed an increase in the phosphorylated form. The remainder showed qualitative shifts to the corresponding embryo-specific proteins ; however, peptide map analyses revealed the existence of common structural units between the corresponding proteins.These modifications were observed in the three species of sea urchin studied (Pseudocentrotu,y depressus, Hemicentrotus pulcherrirnus and Anthocidaris crassispina), except in the case of one protein (L31). Purification of ribosomes by different procedures based on high-salt treatment gave the same results with respect to the egg-specific and embryo-specific proteins.The rapid and large increase in protein synthesis in sea urchin eggs following fertilization is thought to be due to an increase in the availability of maternal mRNA [l -31. Using techniques both in vivo and in vitro, kinetic analyses of a number of components of the translational machinery have been done to find out the mechanism of the 'unmasking' and active utilization of the stored mRNA. However, since numerous parameters are varied under the conditions of cellfree translation systems, there have been conflicting reports concerning the translational activity of ribosomes isolated from eggs and embryos [4-61 and the template activity of masked maternal mRNAs [7,8].Although data on the structural components of ribosomes of sea urchin eggs and embryos are critical for investigating the control mechanism of protein synthesis, very little is known about these subjects. Our previous papers reported the characterization [9] and comparison of species specificity [lo] of the ribosomal proteins of sea urchin eggs. The present study compares the ribosomal proteins of eggs with those of embryos using two-dimensional polyacrylamide gel electrophoresis.To identify the essential variables between egg and embryo ribosomes, we analyzed the ribosomes from (a) unfertilized eggs and embryos at various stages of development, (b) mixtures of unfertilized and fertilized eggs, and (c) three species of sea urchin which have been found to exhibit speciesspecificity in the 60s ribosomal proteins [lo]. We also adopted the fingerprint analysis of tryptic peptides of 'Z51-labeled polypeptides to prove protein identity. EXPERIMENTAL PROCEDURES Eggs and embryosGametes from three species of sea urchin, Pseudocentrotus depressus, Hemicentrotus pulcherrimus and Anthociduris crasThis is the third paper of a series; the first two papers appeared Abbreuiations. SDS, sodium dodecyl sulfate ; mRNPs, messenger el...

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Yeast ribosomal proteins

Cited by 50 publications

References 35 publications

Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae

Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae

The primary structure of protein 44 from the large subunit of yeast ribosomes

Modification of ribosomal proteins in sea urchin eggs following fertilization

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