Nucleic Acids Research, 1981, Vol. 9, No. 7 1643-1656
© 1981
MOLECULAR BIOLOGY |
ATP/Mg++-dependent cross-linking of cap binding proteins to the 5' end of eukaryotic mRNA
Department of Biochemistry, McGill University, Mclntyre Medical Sciences Building 3655 Drummond Street, Montreal, Quebec, Canada H3G 1Y6
Received December 10, 1980. Two proteins of apparent molecular weights of 28,000 and 50,000 daltons were shown to recognize and cross-link specifically to the 5' cap end of oxidized reovirus mRNA. Cross-linking of these proteins to mRNA was ATP/Mg'' dependent, in sharp contrast to cross-linking of a 24K cap binding protein which was purified and characterized previously (Sonenberg, N., Rupprecht, K.M., Hecht, S.M. and Shatkin, A.J. (1979) Proc. Natl. Acad. Sci. USA 76, 4345-4349). Non-hydrolyzable analogues of ATP as well as other nucleotides did not substitute for ATP in the cross-linking reaction and Mg++ was significantly preferred over other divalent cations in cross-linking of the 28K and 50K dalton proteins. A model involving the function of the latter proteins in recognition and unwinding of the 5' end structure of capped eu-karyotic mRNAs is suggested.
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