Loading...
Please wait, while we are loading the content...
Similar Documents
Functional domains of the heavy metal-responsive transcription regulator MTF-1.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Radtke, Falko Georgiev, Oleg G. Müller, Hanne Brugnera, E. Schaffner, Walter |
| Copyright Year | 1995 |
| Abstract | 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. |
| Starting Page | 532 |
| Ending Page | 537 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/nar/23/12/10.1093/nar/23.12.2277/2/23-12-2277.pdf?Expires=1492528635&Key-Pair-Id=APKAIUCZBIA4LVPAVW3Q&Signature=LwoY1Cj2Swg-fJngu5HRfchEuP911MbdSuUXwhK8ZfLI2VTSo7T0KRWPVVvsGJWfMTNq0O5JPypwRO4KYBVuYKm2hcQM1l0242XIMNBNcaBrlL3SYNv1az2UX6sqir7tZA8kS9Gf0RA7x63HGYuMlMobamgqh6E2LRXuTWdhKW8J286K9euab4zttB7b4Sf2~RY0ygImNn~nyt0xAid5myyPJqtKBP2sXHPQAzOienE9HtUuqKmEKSu0raaBtkbTRNhgbWRxoP9UUQg~0v4he2lL5R-IDilHyhiax9XtuNZgpA-EYxC4TF5aBFfWh0h1nApZ88SShcZETXEPJj981A__ |
| Alternate Webpage(s) | https://watermark.silverchair.com/api/watermark?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAAd4wggHaBgkqhkiG9w0BBwagggHLMIIBxwIBADCCAcAGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQMNG3_cxLZiix8TpenAgEQgIIBkbgxIQgr-OLQXeTvqpa9CrERFzQJyBwSB9fZVKGothi7Nv0reSSj2mTMKv8pIdV_I6kfGPtqnjm3fmiBoWeU1UWdI9xUzD1MQA_B4V7VUD-BDpqdkDDDBXEUWsuFdj2QLaCNznYj29X08bOgBVjBOaVBvHVJ56IUwIxCj04DIlY5xBcd3gcQ7kH04mxGCGcdF0uQs3uAo880czsIxpbNiEWtB4CKAYyPWSm6wievGCDMFo-DeUGxqwPRPzm4AFE9vzuEcPL4ZxiHyputqwaNyuwoPG_bTYNVeTi8SDMQGQktSNHv4-0vF3opDh06UMnc5YTG1o-pqLeagp0CDzGZjdJ3ALZvnWDy_aabdO3V4OZ6RTmJut4zZqyFfGCOIsOLpJ4HYCl19I75m3YjxHGRWlRrignOF3DSRP6h_44nvOuIpCyr-ecZAgeZVTQdqjmaCREP0T8_d67N2E3kWnYgyTxlE21XgBa0Md88Mw5EpDEXFSMC6hngjSnwMpJrvyENsUjXXZ6vx2fSMuNlXDcI3vCW |
| PubMed reference number | 7610056v1 |
| Volume Number | 23 |
| Issue Number | 12 |
| Journal | Nucleic acids research |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Acids Chimera organism Deletion Mutation Heparin, Low-Molecular-Weight Metal Ion Binding Metallothionein Metals Metals, Heavy Proline Proline-Rich Domain Threonine Trans-Activation, Genetic Transcription, Genetic Zinc Fingers dna binding promoter |
| Content Type | Text |
| Resource Type | Article |
