dc.creator | Chachami, G. | en |
dc.creator | Paraskeva, E. | en |
dc.creator | Georgatsou, E. | en |
dc.creator | Bonanou, S. | en |
dc.creator | Simos, G. | en |
dc.date.accessioned | 2015-11-23T10:24:23Z | |
dc.date.available | 2015-11-23T10:24:23Z | |
dc.date.issued | 2005 | |
dc.identifier | 10.1016/j.bbrc.2005.03.193 | |
dc.identifier.issn | 0006-291X | |
dc.identifier.uri | http://hdl.handle.net/11615/26536 | |
dc.description.abstract | Hypoxia-inducible factor 1α (HIF- 1α) is the regulatory Subunit of HIF- 1. the transcriptional activator and key mediator of the cellular response to hypoxia. Regulation of HIF-1α Occurs at multiple levels and involves several different post-translational modifications. In order to examine the importance of these modifications for the basic function Of 111F-1χ we have produced in bacteria recombinant full-length human HIF-1χ using different expression systems. We show that this unmodified form of HIF-1χ is able to form a stable heterodimer with the second Subunit of HIF-1 (HIF-1β or ARNT) when both proteins are co-exprosed in Escherichia coli. Furthermore, this bacterially reconstituted heterodimer exhibits specific DNA-binding activity. These data indicate that posttranslational modification of HIF-1χ is not essential for its interaction with ARNT and DNA, and provide an in vitro system for the characterization of the molecular properties of HIF-1χ. © 2005 Elsevier Inc. All rights reserved. | en |
dc.source | Biochemical and Biophysical Research Communications | en |
dc.source.uri | <Go to ISI>://WOS:000228961000014 | |
dc.subject | hypoxia-inducible factor 1 | en |
dc.subject | HIF-1 alpha | en |
dc.subject | ARNT | en |
dc.subject | bacterial expression | en |
dc.subject | heterodimerization | en |
dc.subject | DNA-binding | en |
dc.subject | HYPOXIA-INDUCIBLE FACTOR-1 | en |
dc.subject | ARNT TRANSCRIPTION FACTOR | en |
dc.subject | GENE-EXPRESSION | en |
dc.subject | UNSTRUCTURED PROTEINS | en |
dc.subject | SIGNAL-TRANSDUCTION | en |
dc.subject | HIF | en |
dc.subject | COMPLEX | en |
dc.subject | ALPHA | en |
dc.subject | O-2 | en |
dc.subject | HYDROXYLATION | en |
dc.subject | Biochemistry & Molecular Biology | en |
dc.subject | Biophysics | en |
dc.title | Bacterially produced human HIF-1 alpha is competent for heterodimerization and specific DNA-binding | en |
dc.type | journalArticle | en |