Acidic proteins from wheat germ ribosomes

Madrzak, Cesary J.; Szybiak, Urszula; Legocki, Andrzej B.

doi:10.1016/0014-5793(79)81350-2

Cited by 5 publications

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References 16 publications

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“…Confirming the importance of these proteins in ribosome function is the ubiquitous presence of similar proteins in all the species so far studied (Vidales et al, 1981a). Proteins with p/s lower than L7 and L12 have been reported in rat liver (Stoffler et al, 1974;Reyes et al, 1977), Artemia salina (Moller et al, 1975), yeast (Kruiswijk & Planta, 1975;Zinker & Warner, 1976;Sanchez-Madrid et al, 1979a;Itoh et al, 1979), Krebs II ascites cells (Leader & Coia, 1977), HeLa cells (Horak & Schiffman, 1977), Drosophila melanogaster (Chooi et al, 1980), rabbit reticulocytes (Howard et al, 1975), wheat germ (Madrzak et al, 1979), mouse myeloma cells (Martini & Kruppa, 1979) (Howard et al, 1976). In some cases, the proteins have been characterized (van Agthoven et al, 1978;Tsurugi et al, 1978) and even sequenced (Itoh, 1981;Lin et al, 1982).…”

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confidence: 80%

Acidic proteins of the large ribosomal subunit in Saccharomyces cerevisiae. Effect of phosphorylation

Fj¹,

Mt²,

Jp³

1984

Biochemistry

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Three strongly acidic proteins with pIs between 3.0 and 3.5 have been detected and purified from an ammonium-ethanol extract of Saccharomyces cerevisiae ribosomes. The three proteins, called L45, L44, and L44', have a similar amino acid composition, but differences were shown by tryptic peptide analysis. Nevertheless, the three polypeptides show total cross-reaction to antisera raised against one of them. Protein L44' is very unstable in the extract when treated at the basic pH 9.2, due to an enzymatic process not yet clarified. When purified, the protein is, however, stable. In solution, the proteins are present as dimers, as verified by ultracentrifugation, column filtration, and photochemical cross-linking. The tendency to dimerization is much lower in the case of protein L44'. On the average, 3.2 copies of these proteins are detected per ribosome. The proteins are monophosphorylated when present in the ribosome. Phosphorylation seems to regulate the affinity of the polypeptides for the particles because unphosphorylated proteins bind poorly to the ribosomes deprived of the acidic proteins. Since these proteins are unphosphorylated when present in the cytoplasm [Zinker, S. (1980) Biochim. Biophys. Acta 606, 76-82; Sánchez-Madrid, F., Vidales, F. J., & Ballesta, J. P. G. (1981) Eur. J. Biochem. 114, 609-613], a regulatory mechanism of the ribosomal function based on a phosphorylation-dephosphorylation process of the acidic proteins is being studied.

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mentioning

confidence: 80%

Acidic proteins of the large ribosomal subunit in Saccharomyces cerevisiae. Effect of phosphorylation

Fj¹,

Mt²,

Jp³

1984

Biochemistry

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Chemical components

Bielka¹

1982

The Eukaryotic Ribosome

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Ribosomal acidic proteins of eucaryotic cells

1983

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By the method of ethanol-salt extraction with ion-exchange chromatography on CM-cellulose an acidic protein of pea 80S ribosomes was isolated. This protein located in the large subunit, had a molecular weight of 14 000 and an IEP of 4.7. The protein is partially phosphorylated, alanine-rich and has methionine at the N-terminal position. Based on these characteristics and on the comparative study of tryptic hydrolyzates of the plant protein and E. coli L7/L12, the protein so obtained is found to be homologous to the L7/L12 of the procaryotic ribosomes.

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Acidic proteins from wheat germ ribosomes

Cited by 5 publications

References 16 publications

Acidic proteins of the large ribosomal subunit in Saccharomyces cerevisiae. Effect of phosphorylation

Acidic proteins of the large ribosomal subunit in Saccharomyces cerevisiae. Effect of phosphorylation

Chemical components

Ribosomal acidic proteins of eucaryotic cells

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