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Inhibition of AP-1 DNA binding by nitric oxide involving conserved cysteine residues in Jun and Fos
Department of Medical Biochemistry and Biophysics, Karolinska Institute, Sweden.
Department of Medical Biochemistry and Biophysics, Karolinska Institute, Sweden.
Department of Biosciences at Novum, Karolinska Institute, Huddinge, Sweden.
1998 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 242, no 1, 109-112 p.Article in journal (Refereed) Published
Abstract [en]

Nitric oxide (NO), which has diverse biological effects, can modulate AP-1 activity. Since DNA binding of Jun-Jun and Jun-Fos dimers is regulated in vitro by redox control involving conserved cysteines, we hypothesized that the action of NO is mediated via these residues. We performed electrophoretic mobility-shift analyses using Jun and Fos recombinant proteins and NO solutions. Cysteine-to-serine mutants showed that the inhibition of AP-1 activity following NO treatment was dependent on the presence of Cys7272 and Cys154 in the DNA binding domain of Jun and Fos, respectively. The inhibitory effect of NO was reversed by DTT and the thioredoxin system. Our results demonstrate that NO mediates its inhibitory effect by reacting specifically with the conserved cysteine residues in Jun and Fos.

Place, publisher, year, edition, pages
Elsevier, 1998. Vol. 242, no 1, 109-112 p.
National Category
Medical and Health Sciences
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URN: urn:nbn:se:liu:diva-98836DOI: 10.1006/bbrc.1997.7930PubMedID: 9439619OAI: oai:DiVA.org:liu-98836DiVA: diva2:655979
Available from: 2013-10-14 Created: 2013-10-14 Last updated: 2017-12-06Bibliographically approved

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Spyrou, Giannis

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