English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/81305
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Analysis of HIF-prolyl hydroxylases binding to substrates

AuthorsLandázuri, Manuel O.; Vara-Vega, Alicia; Vitón, Mariano; Cuevas, Yolanda; Peso, Luis del
Issue Date2006
PublisherElsevier
CitationBiochemical and Biophysical Research Communications 351(2): 313-320 (2006)
AbstractHypoxia inducible transcription factors (HIF) are mainly regulated by a group of proline hydroxylases (EGLNs) that, in the presence of oxygen, target HIF for degradation. HIFα contains two independent oxygen degradation domains (N-ODD and C-ODD) that are substrates for these enzymes. In this work, we employed the yeast two-hybrid assay to study the sequence determinants required for the binding of EGLN1 and 3 to HIF1α in a cellular context. Our results demonstrate that, while EGLN1 is able to recognize both ODDs within full length HIF1α protein, EGLN3 only binds to CODD. The analysis of the residue substitutions within CODD uncovered novel critical determinants for EGLN1 and 3 binding. In addition, our results show that both enzymes have a very similar, albeit not identical, residue preference at specific positions in their substrate sequences. © 2006 Elsevier Inc. All rights reserved.
URIhttp://hdl.handle.net/10261/81305
DOI10.1016/j.bbrc.2006.09.170
Identifiersdoi: 10.1016/j.bbrc.2006.09.170
issn: 0006-291X
Appears in Collections:(IIBM) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.