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- Ferreira, Monica ESödertörns högskola,Institutionen för livsvetenskaper,Karolinska Institutet (author)
Mechanism of transcription factor recruitment by acidic activators
- Article/chapterEnglish2005
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- 2005
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- LIBRIS-ID:oai:DiVA.org:sh-14456
- https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-14456URI
- https://doi.org/10.1074/jbc.M502627200DOI
- http://kipublications.ki.se/Default.aspx?queryparsed=id:1955839URI
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- Language:English
- Summary in:English
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- Many transcriptional activators are intrinsically unstructured yet display unique, defined conformations when bound to target proteins. Target-induced folding provides a mechanism by which activators could form specific interactions with an array of structurally unrelated target proteins. Evidence for such a binding mechanism has been reported previously in the context of the interaction between the cancer-related c-Myc protein and the TATA-binding protein, which can be modeled as a two-step process in which a rapidly forming, low affinity complex slowly converts to a more stable form, consistent with a coupled binding and folding reaction. To test the generality of the target-induced folding model, we investigated the binding of two widely studied acidic activators, Gal4 and VP16, to a set of target proteins, including TATA-binding protein and the Swi1 and Snf5 subunits of the Swi/Snf chromatin remodeling complex. Using surface plasmon resonance, we show that these activator-target combinations also display bi-phasic kinetics suggesting two distinct steps. A fast initial binding phase that is inhibited by high ionic strength is followed by a slow phase that is favored by increased temperature. In all cases, overall affinity increases with temperature and, in most cases, with increased ionic strength. These results are consistent with a general mechanism for recruitment of transcriptional components to promoters by naturally occurring acidic activators, by which the initial contact is mediated predominantly through electrostatic interactions, whereas subsequent target-induced folding of the activator results in a stable complex.
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- Hermann, StefanSödertörns högskola,Institutionen för livsvetenskaper,Karolinska Institutet(Swepub:sh)SHSNHN (author)
- Prochasson, PKarolinska Institutet (author)
- Workman, J LStowers Institute for Medical Research, Kansas City, USA (author)
- Berndt, Kurt DSödertörns högskola,Institutionen för livsvetenskaper,Karolinska Institutet(Swepub:sh)SHKTBT (author)
- Wright, Athony P HSödertörns högskola,Institutionen för livsvetenskaper,Karolinska Institutet(Swepub:sh)SHAYWT (author)
- Södertörns högskolaInstitutionen för livsvetenskaper (creator_code:org_t)
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- In:Journal of Biological Chemistry280:23, s. 21779-217840021-92581083-351X
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