13C Relaxation and Dynamics of the Purine Bases in the Iron Responsive Element RNA Hairpin†

Biochemistry ◽  
1998 ◽  
Vol 37 (26) ◽  
pp. 9323-9332 ◽  
Author(s):  
Kathleen B. Hall ◽  
Changguo Tang
Keyword(s):  
Purine Bases ◽  
Iron Responsive Element ◽  
Responsive Element ◽  
Rna Hairpin ◽  
13C Relaxation

A Model of the Iron Responsive Element RNA Hairpin Loop Structure Determined from NMR and Thermodynamic Data†

Biochemistry ◽  
1996 ◽  
Vol 35 (42) ◽  
pp. 13586-13596 ◽  
Author(s):  
Lance G. Laing ◽  
Kathleen B. Hall
Keyword(s):  
Thermodynamic Data ◽  
Loop Structure ◽  
Hairpin Loop ◽  
Iron Responsive Element ◽  
Responsive Element ◽  
Rna Hairpin

scholarly journals Iron-responsive element-binding protein. Phosphorylation by protein kinase C.

1993 ◽  
Vol 268 (36) ◽  
pp. 27363-27370
Author(s):  
R S Eisenstein ◽  
P T Tuazon ◽  
K L Schalinske ◽  
S A Anderson ◽  
J A Traugh
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Binding Protein ◽  
Iron Responsive Element ◽  
Kinase C ◽  
Element Binding Protein ◽  
Responsive Element

scholarly journals Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation.

1992 ◽  
Vol 267 (34) ◽  
pp. 24466-24470 ◽  
Author(s):  
C.K. Tang ◽  
J Chin ◽  
J.B. Harford ◽  
R.D. Klausner ◽  
T.A. Rouault
Keyword(s):  
Binding Protein ◽  
Iron Responsive Element ◽  
Element Binding Protein ◽  
Responsive Element

scholarly journals Loss of park7 activity has differential effects on expression of iron responsive element (IRE) gene sets in the brain transcriptome in a zebrafish model of Parkinson’s disease

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Hui Yung Chin ◽  
Michael Lardelli ◽  
Lyndsey Collins-Praino ◽  
Karissa Barthelson
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Protein Function ◽  
Bioinformatic Analysis ◽  
Zebrafish Model ◽  
Iron Responsive Element ◽  
Brain Transcriptome ◽  
Gene Sets ◽  
Oxidative Phosphorylation Pathway ◽  
Responsive Element

AbstractMutation of the gene PARK7 (DJ1) causes monogenic autosomal recessive Parkinson’s disease (PD) in humans. Subsequent alterations of PARK7 protein function lead to mitochondrial dysfunction, a major element in PD pathology. Homozygous mutants for the PARK7-orthologous genes in zebrafish, park7, show changes to gene expression in the oxidative phosphorylation pathway, supporting that disruption of energy production is a key feature of neurodegeneration in PD. Iron is critical for normal mitochondrial function, and we have previously used bioinformatic analysis of IRE-bearing transcripts in brain transcriptomes to find evidence supporting the existence of iron dyshomeostasis in Alzheimer’s disease. Here, we analysed IRE-bearing transcripts in the transcriptome data from homozygous park7−/− mutant zebrafish brains. We found that the set of genes with “high quality” IREs in their 5′ untranslated regions (UTRs, the HQ5′IRE gene set) was significantly altered in these 4-month-old park7−/− brains. However, sets of genes with IREs in their 3′ UTRs appeared unaffected. The effects on HQ5′IRE genes are possibly driven by iron dyshomeostasis and/or oxidative stress, but illuminate the existence of currently unknown mechanisms with differential overall effects on 5′ and 3′ IREs.

An IRP-like protein from Plasmodium falciparum binds to a mammalian iron-responsive element

Blood ◽  
2001 ◽  
Vol 98 (8) ◽  
pp. 2555-2562 ◽  
Author(s):  
Mark Loyevsky ◽  
Timothy LaVaute ◽  
Charles R. Allerson ◽  
Robert Stearman ◽  
Olakunle O. Kassim ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Regulatory Protein ◽  
Protein S ◽  
Fold Increase ◽  
Binding Activity ◽  
Mobility Shift ◽  
Iron Responsive Element ◽  
Element Binding Protein ◽  
Responsive Element ◽  
Electrophoretic Mobility Shift Assays

Abstract This study cloned and sequenced the complementary DNA (cDNA) encoding of a putative malarial iron responsive element-binding protein (PfIRPa) and confirmed its identity to the previously identified iron-regulatory protein (IRP)–like cDNA from Plasmodium falciparum. Sequence alignment showed that the plasmodial sequence has 47% identity with human IRP1. Hemoglobin-free lysates obtained from erythrocyte-stage P falciparum contain a protein that binds a consensus mammalian iron-responsive element (IRE), indicating that a protein(s) with iron-regulatory activity was present in the lysates. IRE-binding activity was found to be iron regulated in the electrophoretic mobility shift assays. Western blot analysis showed a 2-fold increase in the level of PfIRPa in the desferrioxamine-treated cultures versus control or iron-supplemented cells. Malarial IRP was detected by anti-PfIRPa antibody in the IRE-protein complex fromP falciparum lysates. Immunofluorescence studies confirmed the presence of PfIRPa in the infected red blood cells. These findings demonstrate that erythrocyte P falciparum contains an iron-regulated IRP that binds a mammalian consensus IRE sequence, raising the possibility that the malaria parasite expresses transcripts that contain IREs and are iron-dependently regulated.

scholarly journals Sequence and expression of the murine iron-responsive element binding protein

1991 ◽  
Vol 19 (22) ◽  
pp. 6333-6333 ◽  
Author(s):  
Caroline C. Philpott ◽  
Tracey A. Rouault ◽  
Richard D. Klausner
Keyword(s):  
Binding Protein ◽  
Iron Responsive Element ◽  
Element Binding Protein ◽  
Responsive Element
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