| pubmed-article:19443451 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19443451 | lifeskim:mentions | umls-concept:C0812281 | lld:lifeskim |
| pubmed-article:19443451 | lifeskim:mentions | umls-concept:C0049308 | lld:lifeskim |
| pubmed-article:19443451 | lifeskim:mentions | umls-concept:C0114612 | lld:lifeskim |
| pubmed-article:19443451 | lifeskim:mentions | umls-concept:C2755352 | lld:lifeskim |
| pubmed-article:19443451 | lifeskim:mentions | umls-concept:C0175921 | lld:lifeskim |
| pubmed-article:19443451 | lifeskim:mentions | umls-concept:C1548602 | lld:lifeskim |
| pubmed-article:19443451 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:19443451 | pubmed:dateCreated | 2009-7-27 | lld:pubmed |
| pubmed-article:19443451 | pubmed:abstractText | Arabidopsis ROS1 belongs to a family of plant 5-methycytosine DNA glycosylases that initiate DNA demethylation through base excision. ROS1 displays the remarkable capacity to excise 5-meC, and to a lesser extent T, while retaining the ability to discriminate effectively against C and U. We found that replacement of the C5-methyl group by halogen substituents greatly decreased excision of the target base. Furthermore, 5-meC was excised more efficiently from mismatches, whereas excision of T only occurred when mispaired with G. These results suggest that ROS1 specificity arises by a combination of selective recognition at the active site and thermodynamic stability of the target base. We also found that ROS1 is a low-turnover catalyst because it binds tightly to the abasic site left after 5-meC removal. This binding leads to a highly distributive behaviour of the enzyme on DNA substrates containing multiple 5-meC residues, and may help to avoid generation of double-strand breaks during processing of bimethylated CG dinucleotides. We conclude that the biochemical properties of ROS1 are consistent with its proposed role in protecting the plant genome from excess methylation. | lld:pubmed |
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| pubmed-article:19443451 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19443451 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19443451 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19443451 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19443451 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:19443451 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:19443451 | pubmed:author | pubmed-author:ArizaRafael... | lld:pubmed |
| pubmed-article:19443451 | pubmed:author | pubmed-author:Roldán-Arjona... | lld:pubmed |
| pubmed-article:19443451 | pubmed:author | pubmed-author:Ponferrada-Ma... | lld:pubmed |
| pubmed-article:19443451 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19443451 | pubmed:volume | 37 | lld:pubmed |
| pubmed-article:19443451 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19443451 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19443451 | pubmed:pagination | 4264-74 | lld:pubmed |
| pubmed-article:19443451 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:19443451 | pubmed:meshHeading | pubmed-meshheading:19443451... | lld:pubmed |
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| pubmed-article:19443451 | pubmed:meshHeading | pubmed-meshheading:19443451... | lld:pubmed |
