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Mechanism of transc...
Mechanism of transcription factor recruitment by acidic activators
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- Ferreira, Monica E (författare)
- Södertörns högskola,Institutionen för livsvetenskaper,Karolinska Institutet
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- Hermann, Stefan (författare)
- Södertörns högskola,Institutionen för livsvetenskaper,Karolinska Institutet
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- Prochasson, P (författare)
- Karolinska Institutet
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- Workman, J L (författare)
- Stowers Institute for Medical Research, Kansas City, USA
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- Berndt, Kurt D (författare)
- Södertörns högskola,Institutionen för livsvetenskaper,Karolinska Institutet
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- Wright, Athony P H (författare)
- Södertörns högskola,Institutionen för livsvetenskaper,Karolinska Institutet
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(creator_code:org_t)
- 2005
- 2005
- Engelska.
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 280:23, s. 21779-21784
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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http://kipublication...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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