Abstract
Pyruvate kinase subunits of red cells and liver differ in their molecular weights. Peptide mapping of the rat enzymes has shown that this difference is due to a single exon peptide present in the red cell enzyme1‐3. There is strong genetic evidence in man that both enzymes are encoded by the same structural gene (refs 4–8 and G. E. J. Staal et al., personal communication). Here we describe in vitro protein synthesis experiments using RNA extracted from rat red cells and liver which demonstrate that the difference is reflected in tissue-specific mRNAs. Thus the difference is not due to post-translational processing and presumably involves either gene rearrangement or differential processing of a common nuclear RNA precursor.
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Cleveland, D. W., Fisher, S. G., Kirschner, M. W. & Laemmli, U. K. J. biol. Chem. 252, 1102–1106 (1977).
Harada, K., Saheki, S., Wada, K. & Tanaka, T. Biochim. biophys. Acta 524, 327–339 (1978).
Saheki, S., Saheki, K. & Tanaka, T. FEBS Lett. 93, 25–28 (1978).
Bigley, R. H. & Koler, R. D. Ann. hum. Genet. 31, 383–390 (1965).
Kahn, A., Marie, J., Galand, C. & Boivin, P. Scand. J. Haemat. 16, 250–257 (1976).
Nakashima, K. et al. Blood 43, 537–548 (1974).
Nakashima, K. et al. J. Lab. clin. Med. 90, 1012–1020 (1977).
Shinohara, K. et al. Am. J. hum. Genet. 28, 474–481 (1976).
Kahn, A., Marie, J., Garreau, H. & Sprengers, E. D. Biochim. biophys. Acta 523, 59–74 (1978).
Marie, J., Garreau, H. & Kahn, A. FEBS Lett. 78, 91–94 (1977).
Marie, J. & Kahn, A. Biochem. biophys. Res. Commun. 91, 123–129 (1979).
Sprengers, E. D. & Staal, G. E. J. Biochim. biophys. Acta 570, 259–270 (1979).
Kahn, A., Cottreau, D., Daegelen, D. & Dreyfus, J. C. Eur. J. Biochem. 116, 7–12 (1981).
Hunt, T. & Jackson, R. J. in Modem Trends in Human Leukaemia (eds Neth. R., Gallo, R. C., Spiegelman, S. E. & Stohlman, F.) 300–307 (Lehmans, Munich, 1974).
Cox, R. A. Meth. Enzym. 12, 120–129 (1968).
Hicks, J., Strathern, J. & Klar, A. J. S. Nature 282, 478–482 (1979).
Nasmyth, K. A. & Tatchell, K. Cell 19, 753–764 (1980).
Hoeijmakers, J. H. J., Frasch, A. C. C., Bernards, A., Borst, P. & Cross, G. A. M. Nature 284, 78–80 (1980).
Davis, M. M. et al. Nature 283, 733–739 (1980).
Early, P. W., Davis, M. M., Kaback, D. B., Davidson, N. & Hood, L. Proc. natn. Acad. Sci. U.S.A. 76, 857–861 (1979).
Early, P., Huang, H., Davis, M., Calame, K. & Hood, L. Cell 19, 981–992 (1980).
Alt, F. W. et al. Cell 20, 293–301 (1980).
Early, P. et al. Cell 20, 313–319 (1980).
Singer, P. A., Singer, H. H. & Williamson, A. R. Nature 285, 294–300 (1980).
Hagenbüchle, O. et al. Nature 289, 643–646 (1981).
Young, R. A., Hagenbüchle, O. & Schibler, U. Cell 23, 451–458 (1981).
Laemmli, U. K. Nature 227, 680–685 (1970).
Pehlam, H. P. B. & Jackson, R. J. Eur. J. Biochem. 67, 247–256 (1976).
Bonner, W. M. & Laskey, A. R. Eur. J. Biochem. 46, 83–88 (1974).
Laskey, R. A. & Mills, A. D. Eur. J. Biochem. 56, 335–341 (1975).
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Marie, J., Simon, MP., Dreyfus, JC. et al. One gene, but two messenger RNAs encode liver L and red cell L′ pyruvate kinase subunits. Nature 292, 70–72 (1981). https://doi.org/10.1038/292070a0
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DOI: https://doi.org/10.1038/292070a0
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