| pubmed-article:7610056 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7610056 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:7610056 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
| pubmed-article:7610056 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7610056 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7610056 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
| pubmed-article:7610056 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7610056 | lifeskim:mentions | umls-concept:C0439539 | lld:lifeskim |
| pubmed-article:7610056 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7610056 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:7610056 | pubmed:dateCreated | 1995-8-11 | lld:pubmed |
| pubmed-article:7610056 | pubmed:abstractText | Metallothioneins (MTs) constitute a class of low molecular weight, cysteine-rich, metal binding proteins which are regulated at the level of gene transcription in response to heavy metals and other adverse treatments. We have previously cloned a zinc finger factor (MTF-1) that binds specifically to heavy metal-responsive DNA sequence elements in metallothionein promoters and shown that this factor is essential for basal and heavy metal-induced transcription. Here we report that the C-terminal part of MTF-1 downstream of the DNA binding zinc fingers harbours three different transactivation domains, namely an acidic domain, a proline-rich domain and a domain rich in serine and threonine. When fused to the heterologous DNA binding domain of the yeast factor GAL4 these activation domains function constitutively, i.e. transcription of a GAL4-driven reporter gene is not induced by heavy metals. In search of the region(s) responsible for metal induction, external and internal deletion mutations of mouse and human MTF-1 and chimeric variants thereof were tested with a reporter gene driven by a metal-responsive promoter. The N-terminal part of MTF-1 containing the zinc fingers, which are dependent on zinc for efficient DNA binding, can indeed confer a limited (3- to 4-fold) zinc-responsive transcription when fused to the heterologous activation domain of the viral VP16 protein. Another region containing the acidic and proline-rich activation domains also contributes to metal inducibility, but only in the context of intact MTF-1. This indicates that the activity of MTF-1 results from a complex interplay of different functional domains. | lld:pubmed |
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| pubmed-article:7610056 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7610056 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7610056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7610056 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7610056 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7610056 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:7610056 | pubmed:author | pubmed-author:SchaffnerWW | lld:pubmed |
| pubmed-article:7610056 | pubmed:author | pubmed-author:MüllerH PHP | lld:pubmed |
| pubmed-article:7610056 | pubmed:author | pubmed-author:BrugneraEE | lld:pubmed |
| pubmed-article:7610056 | pubmed:author | pubmed-author:GeorgievOO | lld:pubmed |
| pubmed-article:7610056 | pubmed:author | pubmed-author:RadtkeFF | lld:pubmed |
| pubmed-article:7610056 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7610056 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:7610056 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:7610056 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7610056 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7610056 | pubmed:pagination | 2277-86 | lld:pubmed |
| pubmed-article:7610056 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7610056 | pubmed:meshHeading | pubmed-meshheading:7610056-... | lld:pubmed |
| pubmed-article:7610056 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7610056 | pubmed:articleTitle | Functional domains of the heavy metal-responsive transcription regulator MTF-1. | lld:pubmed |
