Affinity purification of a correctly folded fragment of synthetic HIV-1 mRNA using a HIV-1 Rev peptide-ligand.

D. R. Englebretsen, M. J. Scanlon, M. L. West

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Abstract

Formation of a macromolecular complex between the RNA binding protein HIV-1 Rev and HIV-1 mRNA is an essential prerequisite for nuclear export and subsequent expression of HIV-1 mRNA. The arginine rich peptide TRQARRNRRRRWRARQR, corresponding to residues 34-50 of HIV-1 Rev, contains the mRNA binding motif. We prepared a thioether linked Rev34-50-cellulose conjugate to affinity purify a fragment of synthetic mRNA corresponding to the high affinity binding site for Rev. The correctly folded fraction of mRNA (27.5%) was isolated from a crude synthetic mixture.

Original languageEnglish
Pages (from-to)47-50
Number of pages4
JournalBiomedical Peptides, Proteins & Nucleic Acids: Structure, Synthesis & Biological Activity
Volume2
Issue number2
Publication statusPublished - 1 Jan 1996
Externally publishedYes

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