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  • Bergh, F T (author)

Comparison of nucleosome remodeling by the yeast transcription factor Pho4 and the glucocorticoid receptor

  • Article/chapterEnglish2000

Publisher, publication year, extent ...

  • Elsevier BV,2000
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:sh-15755
  • https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-15755URI
  • https://doi.org/10.1074/jbc.275.12.9035DOI
  • http://kipublications.ki.se/Default.aspx?queryparsed=id:1941213URI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Chromatin reorganization of the PHO5 and murine mammary tumor virus (MMTV) promoters is triggered by binding of either Pho4 or the glucocorticoid receptor (GR), respectively. In order to compare the ability of Pho4 and GR to remodel chromatin and activate transcription, hybrid promoter constructs were created by insertion of the MMTV B nucleosome sequence into the PHO5 promoter and then transformed into a yeast strain expressing GR, Activation of either Pho4 (by phosphate depletion) or GR (by hormone addition) resulted in only slight induction of hybrid promoter activity. However, simultaneous activation of both Pho4 and GR resulted in synergistic activation to levels exceeding that of the wild type PHO5 promoter. Under these conditions, Pho4 completely disrupted the nucleosome containing its binding site. In contrast, GR had little effect on the stability of the MMTV B nucleosome. A minimal transactivation domain of the GR fused to the Pho4 DNA-binding domain is capable of efficiently disrupting the nucleosome with a Pho4-binding site, whereas the complementary hybrid protein (Pho4 activation domain, GR DNA-binding domain) does not labilize the B nucleosome. Therefore, we conclude that significant activation by Pho4 requires nucleosome disruption, whereas equivalent transcriptional activation by GR is not accompanied by overt perturbation of nucleosome structure. Our results show that the DNA-binding domains of the two factors play critical roles in determining how chromatin structure is modified during promoter activation.

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Added entries (persons, corporate bodies, meetings, titles ...)

  • Flinn, Elisabeth MSödertörns högskola,Avdelning Naturvetenskap,Karolinska Institute(Swepub:sh)SHEHFN (author)
  • Svaren, J (author)
  • Wright, Anthony PKarolinska Institutet,Södertörns högskola,Avdelning Naturvetenskap,Karolinska Institute(Swepub:sh)SHAYWT (author)
  • Horz, W (author)
  • Södertörns högskolaAvdelning Naturvetenskap (creator_code:org_t)

Related titles

  • In:Journal of Biological Chemistry: Elsevier BV275:12, s. 9035-90420021-92581083-351X

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