Molecular cloning of mouse glycolate oxidase. High evolutionary conservation and presence of an iron-responsive element-like sequence in the mRNA.

Details

Serval ID
serval:BIB_12371
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Molecular cloning of mouse glycolate oxidase. High evolutionary conservation and presence of an iron-responsive element-like sequence in the mRNA.
Journal
Journal of Biological Chemistry
Author(s)
Kohler S.A., Menotti E., Kühn L.C.
ISSN
0021-9258
Publication state
Published
Issued date
1999
Volume
274
Number
4
Pages
2401-2407
Language
english
Abstract
Iron regulatory proteins (IRPs) control the synthesis of several proteins in iron metabolism by binding to iron-responsive elements (IREs), a hairpin structure in the untranslated region (UTR) of corresponding mRNAs. Binding of IRPs to IREs in the 5' UTR inhibits translation of ferritin heavy and light chain, erythroid aminolevulinic acid synthase, mitochondrial aconitase, and Drosophila succinate dehydrogenase b, whereas IRP binding to IREs in the 3' UTR of transferrin receptor mRNA prolongs mRNA half-life. To identify new targets of IRPs, we devised a method to enrich IRE-containing mRNAs by using recombinant IRP-1 as an affinity matrix. A cDNA library established from enriched mRNA was screened by an RNA-protein band shift assay. This revealed a novel IRE-like sequence in the 3' UTR of a liver-specific mouse mRNA. The newly identified cDNA codes for a protein with high homology to plant glycolate oxidase (GOX). Recombinant protein expressed in bacteria displayed enzymatic GOX activity. Therefore, this cDNA represents the first vertebrate GOX homologue. The IRE-like sequence in mouse GOX exhibited strong binding to IRPs at room temperature. However, it differs from functional IREs by a mismatch in the middle of its upper stem and did not confer iron-dependent regulation in cells.
Keywords
Alcohol Oxidoreductases/genetics, Alcohol Oxidoreductases/metabolism, Amino Acid Sequence, Animals, Base Sequence, Catalysis, Cell Line, Cloning, Molecular, Conserved Sequence, DNA, Complementary, Evolution, Molecular, Humans, Iron Regulatory Protein 1, Iron-Regulatory Proteins, Iron-Sulfur Proteins/metabolism, Liver/enzymology, Mice, Molecular Sequence Data, Oxidation-Reduction, RNA Processing, Post-Transcriptional, RNA, Messenger/genetics, RNA-Binding Proteins/metabolism, Rats, Sequence Homology, Amino Acid, Tumor Cells, Cultured
Pubmed
Web of science
Open Access
Yes
Create date
19/11/2007 12:03
Last modification date
20/08/2019 12:40
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