NDLI: Activation of hypoxia-inducible factor 1alpha: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factor.

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Activation of hypoxia-inducible factor 1alpha: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kallio, P. J. Pongratz, I. Gradin, K. Poellinger, L. Mcguire, J.
Description	Author Affiliation: Kallio PJ ( Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institutet, S-171 77 Stockholm, Sweden.);
Abstract	In response to hypoxia the hypoxia-inducible factor-1 (HIF-1) mediates transcriptional activation of a network of genes encoding erythropoietin, vascular endothelial growth factor, and several glycolytic enzymes. HIF-1 consists of a heterodimer of two basic helix-loop-helix PAS (Per/Arnt/Sim) proteins, HIF-1alpha and Arnt. HIF-1alpha and Arnt mRNAs are constitutively expressed and were not altered upon exposure of HeLa or HepG2 cells to hypoxia, suggesting that the activity of the HIF-1alpha-Arnt complex may be regulated by some as yet unknown posttranscriptional mechanism. In support of this model, we demonstrate here that Arnt protein levels were not increased under conditions that induce an hypoxic response in HeLa and HepG2 cells. However, under identical conditions, HIF-1alpha protein levels were rapidly and dramatically up-regulated, as assessed by immunoblot analysis. In addition, HIF-1alpha acquired a new conformational state upon dimerization with Arnt, rendering HIF-1alpha more resistant to proteolytic digestion in vitro. Dimerization as such was not sufficient to elicit the conformational change in HIF-1alpha, since truncated forms of Arnt that are capable of dimerizing with HIF-1alpha did not induce this effect. Moreover, the high affinity DNA binding form of the HIF-1alpha-Arnt complex was only generated by forms of Arnt capable of eliciting the allosteric change in conformation. In conclusion, the combination of enhanced protein levels and allosteric change by dimerization defines a novel mechanism for modulation of transcription factor activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	11
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA-Binding Proteins Metabolism Nuclear Proteins Protein Conformation Receptors, Aryl Hydrocarbon Transcription Factors Animals Aryl Hydrocarbon Receptor Nuclear Translocator Carcinoma, Hepatocellular Cell Hypoxia Cloning, Molecular Biosynthesis Chemistry Dimerization HeLa Cells Helix-Loop-Helix Motifs Hypoxia-Inducible Factor 1 Hypoxia-Inducible Factor 1, Alpha Subunit Liver Neoplasms Mice Models, Structural Mutagenesis Protein Binding Protein Biosynthesis Protein Multimerization RNA, Messenger Recombinant Fusion Proteins Reticulocytes Sequence Deletion Transcription, Genetic Triticum Tumor Cells, Cultured Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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