TAILIEUCHUNG - Báo cáo khoa học: Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains

Factor-inhibiting hypoxia-inducible factor (FIH) is an Fe(II)⁄2-oxogluta-rate-dependent dioxygenase that acts as a negative regulator of the hypoxia-inducible factor (HIF) by catalysing b-hydroxylation of an asparaginyl residue in its C-terminal transcriptional activation domain (CAD). | IFEBS Journal Factor-inhibiting hypoxia-inducible factor FIH catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains Ming Yang1 Rasheduzzaman Chowdhury1 Wei Ge1 Refaat B. Hamed1 2 Michael A. McDonough1 Timothy D. W. Claridge1 Benedikt M. Kessler3 Matthew E. Cockman3 Peter J. Ratcliffe3 and Christopher J. Schofield1 1 Chemistry Research Laboratory and Oxford Centre for Integrative Systems Biology University of Oxford UK 2 Department of Pharmacognosy Assiut University Egypt 3 Henry Wellcome Building for Molecular Physiology University of Oxford UK Keywords 2-oxoglutarate-dependent dioxygenase ankyrin repeat domain factor inhibiting HIF histidinylhydroxylation post-translational hydroxylation Correspondence M. E. Cockman Henry Wellcome Building for Molecular Physiology University of Oxford Oxford OX3 7BN UK Fax 44 1865 287787 Tel 44 1865 287785 E-mail matthew@ These authors contributed equally to this work Re-use of this article is permitted in accordance with the Terms and Conditions set out at http onlineopen OnlineOpen_Terms Received 10 December 2010 revised 13 January 2011 accepted 18 January 2011 doi Factor-inhibiting hypoxia-inducible factor FIH is an Fe II 2-oxogluta-rate-dependent dioxygenase that acts as a negative regulator of the hypoxiainducible factor HIF by catalysing b-hydroxylation of an asparaginyl residue in its C-terminal transcriptional activation domain CAD . In addition to the hypoxia-inducible factor C-terminal transcriptional activation domain HIF-CAD FIH also catalyses asparaginyl hydroxylation of many ankyrin repeat domain-containing proteins revealing a broad sequence selectivity. However there are few reports on the selectivity of FIH for the hydroxylation of specific residues. Here we report that histidinyl residues within the ankyrin repeat domain of tankyrase-2 can be hydroxylated by FIH. NMR and crystallographic analyses show

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