Abstract
Examination of nascent globin peptides accumulatingin vitro during globin synthesis in rabbit reticulocyte lysates was carried out. A view was supported that nonrandom distribution of codons with different usage frequencies in mRNA may determine the messenger's translation kinetics. Regions of reduced translation of α- and β-globin polypeptide chains were localized, and the cotranslational protein-folding model suggested previously was substantiated. An active conjunction of synthesis and folding of proteins was proposed as one of the main destinations of a translation nonuniformity.
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Abraham, A. K., and Pihl, A. (1980).Eur. J. Biochem. 106, 257–262.
Askonas, B. A., and Williamson, A. R. (1967).Cold Spring Harbor Symp. Quant. Biol. 32, 223–231.
Bennetzen, J. L., and Hall, B. D. (1982a).J. Biol. Chem. 257, 3018–3025.
Bennetzen, J. L., and Hall, B. D. (1982b).J. Biol. Chem. 257, 3026–3031.
Bergman, L. W., and Kuehl, W. M. (1979a).J. Biol. Chem. 254, 5690–5694.
Bergman, L. W., and Kuehl, W. M. (1979b).J. Biol. Chem. 254, 8869–8876.
Bergman, L. W., and Kuehl, W. M. (1979c).J. Supramol. Structure 11, 9–24.
Candelas, G. C., Candelas, T., Ortiz, A., and Rodriguez, O. (1983).Biochem. Biophys. Res. Commun. 116, 1033–1038.
Candelas, G. C., Ortiz, A., and Ortiz, N. (1989).Biochem. Cell Biol. 67, 173–176.
Chaney, W. G., and Morris, A. J. (1979).Arch. Biochem. Biophys. 194, 283–291.
Dayhoff, M. O. (1972).Atlas of Protein Sequence and Structure, Vol. 5, Nat. Biomed. Res. Foundation, Silver Springs, Maryland.
Di Segni, G., Rosen, H., and Kaempfer, R. (1979).Biochemistry 18, 2847–2854.
Grosjean, H., and fiers, W. (1982).Gene 18, 199–209.
Gutman, G. A., and Hatfield, G. W. (1989).Proc. Natl. Acad. Sci. USA 86, 3699–3703.
Ikemura, T. (1981).J. Mol. Biol. 151, 389–409.
Ikemura, T. (1982).J. Mol. Biol. 158, 573–597.
Ikemura, T. (1985).J. Mol. Biol. 2, 13–34.
Kiho, Y., and Rich, A. (1964).Proc. Natl. Acad. Sci., USA 51, 111–118.
Kolb, V. A., Kommer, A. A., and Spirin, A. S. (1987).Dokl. Akad. Nauk. SSSR 296, 1497–1501.
Krasheninnikov, I. A., Komar, A. A., and Adzhubei, I. A. (1988).Dokl. Akad. Nauk. SSSR 303, 995–999.
Krasheninnikov, I. A., Komar, A. A., and Adzhubei, I. A. (1989a).Biokhimia (USSR) 54, 187–200.
Krasheninnikov, I. A., Komar, A. A., and Adzhubei, I. A. (1989b).Dokl. Akad. Nauk. SSSR 305, 1006–1012.
Krasheninnikov, I. A., Komar, A. A., and Adzhubei, I. A. (1989c)Molecular Organization of Biological Structures, Int. Symp., Moscow, Abs., Vol. 2, pp. 269.
Lim, V. I. (1978).FEBS Lett. 89, 10–14.
Lizardi, P. M., Mahdavi, V., Shields, D., and Candelas, G. (1979).Proc. Natl. Acad. Sci. USA 76, 6211–6215.
Lodish, H. F., and Jacobsen, M. (1972).J. Biol. Chem. 247, 3622–3629.
Maeda, N., and Fitch, W. M. (1982).J. Biol. Chem. 257, 2806–2815.
Pelham, H. R. B., and Jackson, R. J. (1976).Eur. J. Biochem. 67, 247–252.
Peters, T., and Davidson, L. K. (1982).J. Biol. Chem. 257, 8847–8853.
Pollitt, S., and Zalkin, H. (1983).J. Bacteriology 153, 27–32.
Post, L. E., and Momura, M. (1980).J. Biol. Chem. 255, 4660–4666.
Protzel, A., and Morris, A. J. (1974).J. Biol. Chem. 249, 4594–4600.
Purvis, I. J., Bettany, A. J. E., Santiago, T. C., Coggins, J. R., Duncan, K., Eason, R., and Borwn, A. J. P. (1987).J. Mol. Biol. 193, 413–417.
Randall, L. L., Josefsson, L.-G., and Hardy, S. J. S. (1980).Biochemistry 107, 375–379.
Ryabova, L. A., Selivanova, O. M., Baranov, V. I., Vasiliev, V. I., and Spirin, A. S. (1988).FEBS Lett. 226, 255–260.
Schagger, H., and von Jagow, G. (1987).Anal. Biochem. 166, 368–379.
Sharp, P. M., Tuohy, T. M. F., and Mosurski, K. R. (1986).Nucleic Acids Res. 14, 5125–5143.
Shpaer, E. G. (1985a).Nucleic Acids Res. 13, 275–288.
Shaper, E. G. (1985b).J. Mol. Biol. 188, 555–564.
Shaper, E. G. (1986).Mol. Biologia (USSR) 20, 1299–1304.
Smith, D. W. E. (1975).Science 190, 529–535.
Smith, D. W. E., and McNamara, A. L. (1971).Science 171, 577–579.
Spirin, A. S. (1986). InRibosome Structure and Protein Biosynthesis (King, J., ed.), Benjamin/Cummings Publishing, Menlo Park, California.
Thomas, L. K., Dix, K., and Thompson, R. C. (1988).Proc. Nat. Acad. Sci. USA 85, 4242–4246.
Varenne, S., Knibiehler, M., Cavard, D., Morlon, J., and Lazdunski, C. (1982).J. Mol. Biol. 159, 57–70.
Wolin, S. L., and Walter, P. (1988).EMBO J. 7, 3559–3569.
Woodward, W. R., Adamson, S. D., McQueen, H. M., Larson, J. W., Estvanik, S. M., Wilairat, P., and Herbert, E. (1973).J. Biol. Chem. 248, 1556–1561.
Yarus, M., and Folley, M. S. (1985).J. Mol. Biol. 182, 529–540.
Zipser, D., and Perrin, D. (1963).Cold Spring Harbor Symp. Quant. Biol. 28, 533–537.
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Krasheninnikov, I.A., Komar, A.A. & Adzhubei, I.A. Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model. J Protein Chem 10, 445–453 (1991). https://doi.org/10.1007/BF01025472
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DOI: https://doi.org/10.1007/BF01025472