scholarly journals Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation.

1994 ◽  
Vol 269 (49) ◽  
pp. 30904-30910
Author(s):  
F Samaniego ◽  
J Chin ◽  
K Iwai ◽  
T A Rouault ◽  
R D Klausner
Keyword(s):  
Structure Function ◽  
Molecular Characterization ◽  
Translational Regulation ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Iron Regulatory Protein ◽  
Iron Responsive Element ◽  
Element Binding Protein ◽  
Responsive Element

scholarly journals Cloning of the cDNA encoding an RNA regulatory protein--the human iron-responsive element-binding protein.

1990 ◽  
Vol 87 (20) ◽  
pp. 7958-7962 ◽  
Author(s):  
T. A. Rouault ◽  
C. K. Tang ◽  
S. Kaptain ◽  
W. H. Burgess ◽  
D. J. Haile ◽  
...  
Keyword(s):  
Binding Protein ◽  
Regulatory Protein ◽  
Iron Responsive Element ◽  
Element Binding Protein ◽  
Responsive Element

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

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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