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PMID: 8233801 Published · ppublish English Journal Article

The interaction between the iron-responsive element binding protein and its cognate RNA is highly dependent upon both RNA sequence and structure.

Nucleic acids research ·Vol. 21 ·No. 19 ·1993-09-25 ·Pages 4627-31

Jaffrey SR, Haile DJ, Klausner RD, Harford JB

Abstract

To assess the influence of RNA sequence/structure on the interaction RNAs with the iron-responsive element binding protein (IRE-BP), twenty eight altered RNAs were tested as competitors for an RNA corresponding to the ferritin H chain IRE. All changes in the loop of the predicted IRE hairpin and in the unpaired cytosine residue characteristically found in IRE stems significantly decreased the apparent affinity of the RNA for the IRE-BP. Similarly, alteration in the spacing and/or orientation of the loop and the unpaired cytosine of the stem by either increasing or decreasing the number of base pairs separating them significantly reduced efficacy as a competitor. It is inferred that the IRE-BP forms multiple contacts with its cognate RNA, and that these contacts, acting in concert, provide the basis for the high affinity of this interaction.

MeSH Terms
Base Sequence Binding, Competitive Ferritins/genetics Gene Expression Regulation Homeostasis Iron/metabolism Iron-Regulatory Proteins Molecular Sequence Data Nucleic Acid Conformation Oligonucleotide Probes/chemistry Protein Biosynthesis RNA, Messenger/metabolism RNA-Binding Proteins/metabolism Structure-Activity Relationship
Chemicals
Iron-Regulatory Proteins Oligonucleotide Probes RNA, Messenger RNA-Binding Proteins Ferritins Iron
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Jaffrey S R
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Haile D J
Klausner R D
Harford J B
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1993-09-25
Pages
4627-31
Language
English
Region
England
NLM ID
0411011
PMCID
PMC311201
Subset
IM
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