| pubmed-article:17701549 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C1412729 | lld:lifeskim |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C1426958 | lld:lifeskim |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C1148616 | lld:lifeskim |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C0150312 | lld:lifeskim |
| pubmed-article:17701549 | lifeskim:mentions | umls-concept:C0242414 | lld:lifeskim |
| pubmed-article:17701549 | pubmed:issue | 8-9 | lld:pubmed |
| pubmed-article:17701549 | pubmed:dateCreated | 2007-8-16 | lld:pubmed |
| pubmed-article:17701549 | pubmed:abstractText | The mammalian transcription factor Bach1 functions as a repressor of the enhancers of heme oxygenase-1 (HO-1) gene (Hmox-1) by forming heterodimers with the small Maf proteins such as MafK. The transcription of Hmox-1 is regulated by the substrate of HO-1, heme. Heme induces expression of Hmox-1 in part by inhibiting the binding of Bach1 to the enhancers and inducing the nuclear export of Bach1. A dipeptide motif of cysteine and proline (CP motif) in Bach1 is essential for the heme-mediated regulation. In this study, we show that five molecules of heme bind to Bach1 by the heme-titration assay. The Bach1-heme complex exhibits an absorption spectrum with a major Soret peak at 371 nm and Raman band at 343 cm(-1) in high amounts of heme and a spectrum containing the major Soret peak at 423 nm at low heme concentrations. The spectroscopic characterization indicates that Bach1 has two kinds of heme-binding sites with different coordination structures. Mutagenesis studies have established that four molecules of heme bind to the cysteine residues of four CP motifs in the C terminus of Bach1. These results raise the possibility that two separated activities of Bach1, DNA-binding and nuclear export, are regulated by heme binding at the different CP motifs of Bach1 respectively, but not by cooperative heme-binding. | lld:pubmed |
| pubmed-article:17701549 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17701549 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17701549 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17701549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17701549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17701549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17701549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17701549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17701549 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17701549 | pubmed:issn | 1521-6543 | lld:pubmed |
| pubmed-article:17701549 | pubmed:author | pubmed-author:IgarashiKazuh... | lld:pubmed |
| pubmed-article:17701549 | pubmed:author | pubmed-author:Ikeda-SaitoMa... | lld:pubmed |
| pubmed-article:17701549 | pubmed:author | pubmed-author:TomitaTakeshi... | lld:pubmed |
| pubmed-article:17701549 | pubmed:author | pubmed-author:MatsuiToshita... | lld:pubmed |
| pubmed-article:17701549 | pubmed:author | pubmed-author:HiraShusukeS | lld:pubmed |
| pubmed-article:17701549 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17701549 | pubmed:volume | 59 | lld:pubmed |
| pubmed-article:17701549 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17701549 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17701549 | pubmed:pagination | 542-51 | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:meshHeading | pubmed-meshheading:17701549... | lld:pubmed |
| pubmed-article:17701549 | pubmed:articleTitle | Bach1, a heme-dependent transcription factor, reveals presence of multiple heme binding sites with distinct coordination structure. | lld:pubmed |
| pubmed-article:17701549 | pubmed:affiliation | Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Sendai, Japan. | lld:pubmed |
| pubmed-article:17701549 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17701549 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:17701549 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17701549 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17701549 | lld:pubmed |
