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How transcriptional activators bind target proteins
Södertörn University, Avdelning Naturvetenskap.
Södertörn University, Avdelning Naturvetenskap.ORCID iD: 0000-0002-3049-967X
Södertörn University, Avdelning Naturvetenskap.
2001 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 276, no 43, 40127-40132 p.Article in journal (Refereed) Published
Abstract [en]

The product of the proto-oncogene c-myc influences many cellular processes through the regulation of specific target genes. Through its transactivation domain (TAD), c-Myc protein interacts with several transcription factors, including TATA-binding protein (TBP). We present data that suggest that in contrast to some other transcriptional activators, an extended length of the c-Myc TAD is required for its binding to TBP. Our data also show that this interaction is a multistep process, in which a rapidly forming low affinity complex slowly converts to a more stable form. The initial complex formation results from ionic or polar interactions, whereas the slow conversion to a more stable form is hydrophobic in nature. Based on our results, we suggest two alternative models for activation domain/target protein interactions, which together provide a single universal paradigm for understanding activator-target factor interactions.

Place, publisher, year, edition, pages
2001. Vol. 276, no 43, 40127-40132 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:sh:diva-15842DOI: 10.1074/jbc.M103793200ISI: 000171789200084PubMedID: 11514548ScopusID: 2-s2.0-0035955635OAI: diva2:509054
Available from: 2012-03-12 Created: 2012-03-09 Last updated: 2016-01-11Bibliographically approved

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Hermann, StefanBerndt, Kurt DWright, Anthony P H
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