Ballinger, D. G., & Pardue, M. L. (1983), The control of protein synthesis during heat shock in Drosophila cells involves altered polypeptide elongation rates," Cell 33: 103-114.

Candelas, G. C., Carrasco, C. E., Dompenciel, R. E., Arroyo, G., & Candelas, T. M. (1987), Strategies of fibroin production. In Translational Regulation of Gene Expression (J. Ilan, ed.), p.p. 209-228. New York, Plenum Press.

Chaney, W. G., & Morris, A. J. (1979), Nonuniform size distribution of nascent peptides. The effect of messenger RNA structure upon the rate of translation. Arch. Biochem. Biophys. 194: 283-291.

Chavancy, G., Marbaix, G, Huez, G., & Cleuter, Y. (1981), Effect of tRNA pool balance on rate and uniformity of elongation during translation of fibroin mRNA in a reticulocyte cell-free system. Biochimie 63: 611-618.

Chen, G. T., & Inouye, M. (1990), Suppression of the negative effects of minor arginine codons on gene expression: preferential usage of minor codons within the first 25 codons of the Escherichia coli genes. Nucleic Acids Res. 18: 1465-1473.

Collier, R. J. (1975), Diphtheria toxin: Mode of action and structure. Bact. Rev. 39:54-85.

Elska, A., Matsuka, G., Matiash, U., Nasarenko, I., & Semenova, N. (1971), tRNA and aminoacyl-tRNA synthetases during differentiation and various functional states of the mammary gland. Biochim. Biophys. Acta 247: 430-440.

Endo, Y., & Wool, I. (1982), The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence of the alpha-sarcin cleavage site in 28S ribosomal ribonucleic acid. J. Biol. Chem. 257, 9054-9060.

Endo, Y., Mitsui, K., Motizuki, M., & Tsurugi, K. (1987), The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28S ribosomal RNA caused by the toxins. J. Biol. Chem. 262, 5908-5912.

Endo, Y., Tsurugi, K., Yutsudo, T., Takeda, Y., Ogasawara, T., & Igarashi, K. (1988), Site of action of a Vero toxin (VT2) from Escherichia coli 0157:H7 and of Shiga toxin on eukaryotic ribosomes. Eur. J. Biochem. 171: 45-50.

Endo, Y., & Wool, I. (1982), The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence of the alpha-sarcin cleavage site in 28S ribosomal ribonucleic acid. J. Biol. Chem. 257: 9054-9060.

Furutani, M., Kashiwagi, K., Ito, K., Endo, Y., & Igarashi, K., (1992), Comparison of the modes of action of a Vero toxin (a Shiga-like toxin) from Escherichia coli, of ricin, and of alpha-sarcin. Arch. Biochem. Biophys. 293: 140146.

Garel, J.-P. (1976), Quantitative adaptation of isoacceptor tRNAs to mRNA codons of alanine, glycine, and serine. Nature 260: 805-806.

Gehrke, L., Bast, R. E., & Ilan, J. (1981), An analysis of rates of polypeptide chain elongation in avian liver explants following in vivo estrogen treatment. II. Determination of the specific rates of elongation of serum albumin and vitellogenin nascent chains. J. Biol. Chem. 256: 2522-2530.

Grosjean, H., & Fiers, W. (1982), Preferential codon usage in prokaryotic genes: The optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Gene 18:199-209.

Gu, Z., Harrod, R., Rogers, E. J., & Lovett, P. S. (1994), Anti-peptidyl transferase leader peptides of attenuation-regulated chloramphenicol-resistance genes. Proc. Natl. Acad. Sci. U.S.A. 91: 5612-5616.

van Heyningen, S. (1980), ADP-ribosylation by bacterial toxins. In The Enzymology of Post-Translational Modification of Proteins (R. B. Freedman and H. C. Hawkins, eds.), vol. 1, p.p. 387-422. Academic Press, London.

Ikemura, T. (1981), Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes. J. Mol. Biol. 146: 1-21.

Kao, R., & Davies, J. (1995), Fungal ribotoxins: a family of naturally engineered targeted toxins? In Frontiers in Translation (Matheson, A. T., Davies, J. E., Dennis, P. P., & Hill, W. E., eds.), Biochem. Cell Biol. 73: 1151-1159.

Kim, J., Klein, P. G., & Mullet, J. E. (1991), Ribosomes pause at specific sites during synthesis of membrane-bound chloroplast reaction center protein D1. J. Biol. Chem. 266: 14931-14938.

Komar, A. A., & Jaenicke, R. (1995), Kinetics of translation of gamma-B crystallin and its circularly permutated variant in an in vitro cell-free system: Possible relations to codon distribution and protein folding. FEBS Letters 376: 195-198.

Krasheninnikov, I. A., Komar, A. A., & Adzhubei, I. A. (1991), Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model. J. Protein Chem. 10: 445-453.

Lawrence, J. B., & Singer, R. H. (1986), Intracellular localization of messenger RNAs for cytoskeletal proteins. Cell 45: 407-415.

Lizardi, P. M., Mahdavi, V., Shields, D., & Candelas, G. (1979), Discontinuous translation of silk fibroin in a reticulocyte cell-free system and in intact silk gland cells. Proc. Natl. Acad. Sci. USA 76: 6211-6215.

Nairn, A. C., & Palfrey, H. C. (1987), Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor 2. J. Biol. Chem. 262: 17299-17303.

Nairn, A. C., & Palfrey, H. C. (1996), Regulation of protein synthesis by calcium. In Translational Control (Hershey, J. W, B., Mathews, M. B., & Sonenberg, N., eds.), p.p. 295-318. CSHL Press.

Nielsen, P. J., & McConkey, E. H. (1980), Evidence for control of protein synthesis in HeLa cells via the elongation rate. J. Cell Physiol. 104: 269-281.

Nygard, O., & Nilsson, L. (1985), Reduced ribosomal binding of eukaryotic elongation factor 2 following ADP-ribosylation. Difference in binding selectivity between polyribosomes and reconstituted monoribosomes. Biochim. Biophys. Acta 824: 152-162.

Obrig, T. G., Moran, T. P., & Brown, J. E. (1987), The mode of action of Shiga toxin on peptide elongation of eukaryotic protein synthesis. Biochem. J. 244: 287-294.

Olsnes, S., & Pihl, A. (1982a), Toxic lectins and related proteins. In Molecular Actions of Toxins and Viruses (P. Cohen & S. van Heyningen, eds.), p.p. 51-105., Elsevier/North-Holland, Amsterdam.

Olsnes, S., & Pihl, A. (1982b), Chimeric toxins. Pharmac. Ther. 15: 355-381.

Pappenheimer, A. M. (1977), Diphtheria toxin. Ann. Rev. Biochem. 46: 69-94.

Protzel, A., & Morris, A. J. (1974), Gel chromatographic analysis of nascent globin chains. Evident of nonuniform size distribution. J. Biol. Chem. 249: 4594-4600.

Pulkrabek, P., & Rychlik, I. (1968), Effect of univalent cations and role of GTP and supernatant factors during biosynthesis of polylysine chain. Biochim. Biophys. Acta 155: 219-227.

Rebagliati, M. R., Weeks, D. L., Harvey, R. P., & Melton, D. A. (1985), Identification and cloning of localized maternal RNAs fromXenopus eggs. Cell 42: 769-777.

Rosenberg, A. H., Goldman, E., Dunn, J. J., Studier, F. W., & Zubay, G. (1993), Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system. J. Bact. 175: 716-722.

Ryazanov, A. G. (1987), Ca2+/calmodulin-dependent phosphorylation of elongation factor 2. FEBSLetters 214: 331334.

Ryazanov, A. G., & Davydova, E. K. (1989), Mechanism of elongation factor 2 (EF-2) inactivation upon phosphorylation. Phosphorylated EF-2 is unable to catalyze translocation. FEBS Letters 251:187-190.

Ryazanov, A. G., Ovchinnikov, L. P, & Spirin, A. S. (1987), Development of structural organization of protein-synthesizing machinery from prokaryotes to eukaryotes. BioSystems 20: 275-288.

Ryazanov, A. G., Shestakova, E. A., & Natapov, P. G. (1988), Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation. Nature 334: 170-173.

Spanjaard, R. A., & van Duin, J. (1988), Translation of the sequence AGG-AGG yields 50% ribosomal frameshift. Proc. Natl. Acad. Sci. USA 85: 7967-7971.

Spirin, A. S., & Ryazanov, A. G. (1991), Regulation of elongation rate. In Translation in Eukaryotes (H. Trachsel, ed.), p.p. 325-350. CRC Press, Boca Raton, Florida.

Svitkin, Yu. V., & Agol, V. I. (1983), Translational barrier in central region of encephalomyocarditis virus genome. Modulation by elongation factor 2 (eEF-2). Eur. J. Biochem. 133: 145-154.

Theodorakis, N. G., Banerji, S. S., & Morimoto, R. I. (1988), HSP70 mRNA translation in chicken reticulocytes is regulated at the level of elongation. J. Biol. Chem. 263: 14579-14585.

Wolin, S. L., & Walter, P. (1988), Ribosome pausing and stacking during translation of a eukaryotic mRNA. EMBO J. 7: 3559-3569.

Wolin, S. L., & Walter, P. (1989), Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate. J. Cell Biol. 109: 2617-2622.

Wu, R. S., & Warner, J. R. (1971), Cytoplasmic synthesis of nuclear proteins. Kinetics of accumulation of radioactive proteins in various cell fractions after brief pulses. J. Cell Biol. 51: 643-652.

Young, J. C., & Andrews, D. W. (1996), The signal recognition particle receptor alpha subunit assembles co-translationally on the endoplasmic reticulum membrane during an mRNA-encoded translation pause in vitro. EMBO J. 15: 172-181.

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