| pubmed-article:17060459 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17060459 | lifeskim:mentions | umls-concept:C1333336 | lld:lifeskim |
| pubmed-article:17060459 | lifeskim:mentions | umls-concept:C0145822 | lld:lifeskim |
| pubmed-article:17060459 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:17060459 | lifeskim:mentions | umls-concept:C0002145 | lld:lifeskim |
| pubmed-article:17060459 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:17060459 | lifeskim:mentions | umls-concept:C0301039 | lld:lifeskim |
| pubmed-article:17060459 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17060459 | pubmed:dateCreated | 2006-12-14 | lld:pubmed |
| pubmed-article:17060459 | pubmed:abstractText | Previous studies have demonstrated that the base excision repair enzyme thymine DNA glycosylase (TDG) mediates recruitment of histone acetyltransferases CREB-binding protein (CBP) and p300 to DNA, suggesting a plausible role for these factors in TDG-mediated repair. Furthermore, TDG was found to potentiate CBP/p300-dependent transcription and serve as a substrate for CBP/p300 acetylation. Here, we show that the small ubiquitin-like modifier 1 (SUMO-1) protein binding activity of TDG is essential for activation of CBP and localization to promyelocytic leukemia protein oncogenic domains (PODs). SUMO-1 binding is mediated by two distinct amino- and carboxy-terminal motifs (residues 144 to 148 and 319 to 322) that are negatively regulated by DNA binding via an amino-terminal hydrophilic region (residues 1 to 121). TDG is also posttranslationally modified by covalent conjugation of SUMO-1 (sumoylation) to lysine 341. Interestingly, we found that sumoylation of TDG blocks interaction with CBP and prevents TDG acetylation in vitro. Furthermore, sumoylation effectively abrogates intermolecular SUMO-1 binding and a sumoylation-deficient mutant accumulates in PODs, suggesting that sumoylation negatively regulates translocation to these nuclear structures. These findings suggest that TDG sumoylation promotes intramolecular interactions with amino- and carboxy-terminal SUMO-1 binding motifs that dramatically alter the biochemical properties and subcellular localization of TDG. | lld:pubmed |
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| pubmed-article:17060459 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17060459 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17060459 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17060459 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17060459 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17060459 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:17060459 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:17060459 | pubmed:author | pubmed-author:TiniMarcM | lld:pubmed |
| pubmed-article:17060459 | pubmed:author | pubmed-author:RaoAnitaA | lld:pubmed |
| pubmed-article:17060459 | pubmed:author | pubmed-author:MohanRyan DRD | lld:pubmed |
| pubmed-article:17060459 | pubmed:author | pubmed-author:GagliardiJaso... | lld:pubmed |
| pubmed-article:17060459 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17060459 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:17060459 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17060459 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17060459 | pubmed:pagination | 229-43 | lld:pubmed |
| pubmed-article:17060459 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17060459 | pubmed:meshHeading | pubmed-meshheading:17060459... | lld:pubmed |
| pubmed-article:17060459 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17060459 | pubmed:articleTitle | SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment. | lld:pubmed |
