| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 276, Issue 18, 14791-14796, May 4, 2001
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Department of Pharmacology, University of Minnesota,
Minneapolis, Minnesota 55455-0347
Vertebrates control intracellular iron
concentration principally through the interaction of iron regulatory
proteins with mRNAs that contain an iron responsive element, a
small hairpin with a bulged C. The hairpin loop and bulged C have
previously been assumed to be critical for binding and have been
proposed to make direct contact with the iron regulatory proteins.
However, we show here that a U or G can be substituted for the bulged C provided that specific nucleotides are also present within internal loops. The Kd, IC50 and chemical
modifications of the iron responsive element variants are similar to
the wild-type. Results are more consistent with a role in which the
C-bulge functions to orient the hairpin for optimal protein binding
rather than to directly contact the protein. Characterization of
these novel iron responsive element variants may facilitate the
identification of additional mRNAs whose expression is controlled
by iron regulatory proteins, as well as provide insight into the nature
of a critical RNA-protein interaction.
The Hairpin Loop but Not the Bulged C of the Iron Responsive
Element Is Essential for High Affinity Binding to Iron Regulatory
Protein-1*
and
*
This work was supported by grants from the Minnesota Medical
Foundation and American Heart Association Grant MN 9706286A.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported in part by National Institutes of Health Training Grant T32GM07994.
§
To whom correspondence should be addressed. Tel.: 612-624-3132;
Fax: 612-625-8408; E-mail: gconnell@lenti.med.umn.edu.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  C. O. dos Santos, L. C. Dore, E. Valentine, S. G. Shelat, R. C. Hardison, M. Ghosh, W. Wang, R. S. Eisenstein, F. F. Costa, and M. J. Weiss An Iron Responsive Element-like Stem-Loop Regulates {alpha}-Hemoglobin-stabilizing Protein mRNA J. Biol. Chem., October 3, 2008; 283(40): 26956 - 26964. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Sanchez, B. Galy, T. Dandekar, P. Bengert, Y. Vainshtein, J. Stolte, M. U. Muckenthaler, and M. W. Hentze Iron Regulation and the Cell Cycle: IDENTIFICATION OF AN IRON-RESPONSIVE ELEMENT IN THE 3'-UNTRANSLATED REGION OF HUMAN CELL DIVISION CYCLE 14A mRNA BY A REFINED MICROARRAY-BASED SCREENING STRATEGY J. Biol. Chem., August 11, 2006; 281(32): 22865 - 22874. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. J. Mayo, P. Kohlhepp, D. Zhang, and J. J. Winzerling Effects of sham air and cigarette smoke on A549 lung cells: implications for iron-mediated oxidative damage Am J Physiol Lung Cell Mol Physiol, April 1, 2004; 286(4): L866 - L876. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. R. ALLERSON, A. MARTINEZ, E. YIKILMAZ, and T. A. ROUAULT A high-capacity RNA affinity column for the purification of human IRP1 and IRP2 overexpressed in Pichia pastoris RNA, March 1, 2003; 9(3): 364 - 374. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Erlitzki, J. C. Long, and E. C. Theil Multiple, Conserved Iron-responsive Elements in the 3'-Untranslated Region of Transferrin Receptor mRNA Enhance Binding of Iron Regulatory Protein 2 J. Biol. Chem., November 1, 2002; 277(45): 42579 - 42587. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
