Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro.
In humans, many responses to hypoxia including angiogenesis and erythropoiesis are mediated by the alpha/beta-heterodimeric transcription factor hypoxia inducible factor (HIF). The stability and/or activity of human HIF-1alpha are modulated by post-translational modifications including prolyl and as...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2006
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| _version_ | 1797095954227134464 |
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| author | Murray-Rust, T Oldham, N Hewitson, K Schofield, C |
| author_facet | Murray-Rust, T Oldham, N Hewitson, K Schofield, C |
| author_sort | Murray-Rust, T |
| collection | OXFORD |
| description | In humans, many responses to hypoxia including angiogenesis and erythropoiesis are mediated by the alpha/beta-heterodimeric transcription factor hypoxia inducible factor (HIF). The stability and/or activity of human HIF-1alpha are modulated by post-translational modifications including prolyl and asparaginyl hydroxylation, phosphorylation, and reportedly by acetylation of the side-chain of Lys532 by ARD1 (arrest defective protein 1 homologue), an acetyltransferase. Using purified recombinant human ARD1 (hARD1) we did not observe ARD1-mediated N-acetylation of Lys532 using fragments of HIF-1alpha. However, recombinant hARD1 from Escherichia coli was produced with partial N-terminal acetylation and was observed to undergo slow self-mediated N-terminal acetylation. The observations are consistent with the other data indicating that hARD1, at least alone, does not acetylate HIF-1alpha, and with reports on the N-terminal acetyltransferase activity of a recently reported heterodimeric complex comprising hARD1 and N-acetyltransferase protein. |
| first_indexed | 2024-03-07T04:35:21Z |
| format | Journal article |
| id | oxford-uuid:cfbcdf5e-6eb1-4f56-9f50-fb03503a3110 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:35:21Z |
| publishDate | 2006 |
| record_format | dspace |
| spelling | oxford-uuid:cfbcdf5e-6eb1-4f56-9f50-fb03503a31102022-03-27T07:44:47ZPurified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:cfbcdf5e-6eb1-4f56-9f50-fb03503a3110EnglishSymplectic Elements at Oxford2006Murray-Rust, TOldham, NHewitson, KSchofield, CIn humans, many responses to hypoxia including angiogenesis and erythropoiesis are mediated by the alpha/beta-heterodimeric transcription factor hypoxia inducible factor (HIF). The stability and/or activity of human HIF-1alpha are modulated by post-translational modifications including prolyl and asparaginyl hydroxylation, phosphorylation, and reportedly by acetylation of the side-chain of Lys532 by ARD1 (arrest defective protein 1 homologue), an acetyltransferase. Using purified recombinant human ARD1 (hARD1) we did not observe ARD1-mediated N-acetylation of Lys532 using fragments of HIF-1alpha. However, recombinant hARD1 from Escherichia coli was produced with partial N-terminal acetylation and was observed to undergo slow self-mediated N-terminal acetylation. The observations are consistent with the other data indicating that hARD1, at least alone, does not acetylate HIF-1alpha, and with reports on the N-terminal acetyltransferase activity of a recently reported heterodimeric complex comprising hARD1 and N-acetyltransferase protein. |
| spellingShingle | Murray-Rust, T Oldham, N Hewitson, K Schofield, C Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro. |
| title | Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro. |
| title_full | Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro. |
| title_fullStr | Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro. |
| title_full_unstemmed | Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro. |
| title_short | Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro. |
| title_sort | purified recombinant hard1 does not catalyse acetylation of lys532 of hif 1alpha fragments in vitro |
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