NDLI: The iron-responsive element binding protein: a method for the affinity purification of a regulatory RNA-binding protein.

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The iron-responsive element binding protein: a method for the affinity purification of a regulatory RNA-binding protein.

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The iron-responsive element binding protein: a method for the affinity purification of a regulatory RNA-binding protein.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Haile, D. J. Hentze, M. W. Klausner, R. D. Harford, J. B. Rouault, T. A.
Description	Author Affiliation: Rouault TA ( Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.);
Abstract	A method of affinity purification of a regulatory protein that binds specific RNA sequences is described. RNAs containing the regulatory sequences are transcribed in vitro from oligonucleotide templates, biotinylated, and incubated with unfractionated cytosol. Specific RNA-protein complexes are bound in solution to avidin, and the resulting complex is bound to biotin-agarose beads. The cytosolic binding protein is released from the RNA in high salt, and a second round of purification yields an essentially homogeneous protein. Using this method, we have identified the protein in human liver that binds iron-responsive RNA regulatory sequences. Iron-responsive elements (IREs) are RNA stem-loops present in the mRNAs encoding ferritin and the transferrin receptor. IREs form the basis for the translational regulation of ferritin gene expression and the regulation of transferrin receptor mRNA degradation rates. The IRE binding protein purified by this technique migrates as a 90-kDa polypeptide on SDS/PAGE. The interaction of the purified protein with IRE-containing RNAs can be detected by gel-mobility shift assays or by covalent crosslinking induced by UV irradiation.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carrier Proteins Isolation & Purification Metabolism Genetics Chromatography, Affinity Cross-Linking Reagents Liver Mercaptoethanol Pharmacology Molecular Weight Nucleic Acid Conformation RNA RNA-Binding Proteins Regulatory Sequences, Nucleic Acid Transcription, Genetic Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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