Schlegl J, Gegout V, Schlager B, Hentze M W, Westhof E, Ehresmann C, Ehresmann B, Romby P
Probing the structure of the regulatory region of human transferrin receptor messenger RNA and its interaction with iron regulatory protein-1 Article de journal
Dans: RNA, vol. 3, no. 10, p. 1159-1172, 1997, ISBN: 9326491, (1355-8382 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Base Composition Base Sequence Binding Sites Electrophoresis, Messenger/*chemistry/metabolism RNA-Binding Proteins/*metabolism Receptors, Molecular Molecular Sequence Data Mutation *Nucleic Acid Conformation RNA, Non-U.S. Gov't, Polyacrylamide Gel Ethylnitrosourea/pharmacology Human Hydrolysis Hydroxyl Radical/metabolism Iron/metabolism Iron Regulatory Protein 1 Iron-Regulatory Proteins Iron-Sulfur Proteins/*metabolism Lead/pharmacology Models, ROMBY, Transferrin/*genetics Ribonuclease T1/metabolism Support, Unité ARN
@article{,
title = {Probing the structure of the regulatory region of human transferrin receptor messenger RNA and its interaction with iron regulatory protein-1},
author = {J Schlegl and V Gegout and B Schlager and M W Hentze and E Westhof and C Ehresmann and B Ehresmann and P Romby},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9326491},
isbn = {9326491},
year = {1997},
date = {1997-01-01},
journal = {RNA},
volume = {3},
number = {10},
pages = {1159-1172},
abstract = {A portion of the 3'UTR of the human transferrin receptor mRNA mediates iron-dependent regulation of mRNA stability. The minimal RNA regulatory region contains three conserved hairpins, so-called iron responsive elements (IREs), that are recognized specifically by iron regulatory proteins (IRPs). The structure of this regulatory region and its complex with IRP-1 was probed using a combination of enzymes and chemicals. The data support the existence of an intrinsic IRE loop structure that is constrained by an internal C-G base pair. This particular structure is one of the determinants required for optimal IRP binding. IRP-1 covers one helical turn of the IRE and protects conserved residues in each of the three IREs: the bulged cytosine and nucleotides in the hairpin loops. Two essential IRP-phosphate contacts were identified by ethylation interference. Three-dimensional modeling of one IRE reveals that IRP-1 contacts several bases and the ribose-phosphate backbone located on one face in the deep groove, but contacts also exist with the shallow groove. A conformational change of the IRE loop mediated by IRP-1 binding was visualized by Pb2+-catalyzed hydrolysis. This effect is dependent on the loop structure and on the nature of the closing base pair. Within the regulatory region of transferrin receptor mRNA, IRP-1 induces reactivity changes in a U-rich hairpin loop that requires the presence of the stem-loop structure located just downstream the endonucleolytic cleavage site identified by Binder et al. (Binder R et al. 1994, EMBO J 13:1969-1980). These results provide indications of the mechanism by which IRP-1 stabilizes the transferrin receptor mRNA under iron depletion conditions.},
note = {1355-8382
Journal Article},
keywords = {Base Composition Base Sequence Binding Sites Electrophoresis, Messenger/*chemistry/metabolism RNA-Binding Proteins/*metabolism Receptors, Molecular Molecular Sequence Data Mutation *Nucleic Acid Conformation RNA, Non-U.S. Gov't, Polyacrylamide Gel Ethylnitrosourea/pharmacology Human Hydrolysis Hydroxyl Radical/metabolism Iron/metabolism Iron Regulatory Protein 1 Iron-Regulatory Proteins Iron-Sulfur Proteins/*metabolism Lead/pharmacology Models, ROMBY, Transferrin/*genetics Ribonuclease T1/metabolism Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}