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. 1979 Sep;76(9):4345-9.
doi: 10.1073/pnas.76.9.4345.

Eukaryotic mRNA cap binding protein: purification by affinity chromatography on sepharose-coupled m7GDP

N Sonenberg, K M Rupprecht, S M Hecht, A J Shatkin

Eukaryotic mRNA cap binding protein: purification by affinity chromatography on sepharose-coupled m7GDP

N Sonenberg et al. Proc Natl Acad Sci U S A. 1979 Sep.

Abstract

A 24,000-dalton polypeptide that binds strongly and can be specifically crosslinked to the 5'-terminal cap structure m7GpppN in eukaryotic mRNAs has been detected in protein synthesis initiation factor preparations [Proc. Natl. Acad. Sci. USA (1978) 75, 4843--4847]. This polypeptide has been purified to apparent homogeneity by one chromatographic passage through an affinity resin prepared by coupling the levulinic acid O2',3'-acetal of m7GDP to AH-Sepharose 4B. Translation, in HeLa cell extracts, of capped mRNAs including Sindbis virus, reovirus, and rabbit globin mRNAs was stimulated by the cap-binding protein under conditions that did not increase translation of noncapped RNAs of encephalomyocarditis virus and satellite tobacco necrosis virus.

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References

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