Eukaryotic mRNA cap binding protein

purification by affinity chromatography on sepharose-coupled m7GDP.

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

Research output: Contribution to journalArticle

144 Citations (Scopus)

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
StatePublished - Sep 1979
Externally publishedYes

Fingerprint

RNA Cap-Binding Proteins
Affinity Chromatography
Sepharose
Messenger RNA
Tobacco necrosis satellite virus
Encephalomyocarditis virus
Sindbis Virus
Acetals
Peptide Initiation Factors
Peptides
Globins
RNA Viruses
Cell Extracts
HeLa Cells
Rabbits
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Eukaryotic mRNA cap binding protein : purification by affinity chromatography on sepharose-coupled m7GDP. / Sonenberg, N.; Rupprecht, K. M.; Hecht, Sidney; Shatkin, A. J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 76, No. 9, 09.1979, p. 4345-4349.

Research output: Contribution to journalArticle

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