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

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

Research output: Contribution to journalArticle

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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.

Original languageEnglish (US)
Pages (from-to)4345-4349
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume76
Issue number9
DOIs
StatePublished - Sep 1979

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