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The N-terminal half of the Drosophila Rel/NF-kappa B factor Relish, REL-68, constitutively activates transcription of specific Relish target genes
Stockholm University, Faculty of Science, Department of Molecular Biology and Functional Genomics.
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2009 (English)In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 33, no 5, 690-696 p.Article in journal (Refereed) Published
Abstract [en]

The Rel/NF-kappa B transcription factor Relish is a major regulator of the antimicrobial response in Drosophila. Upon immune challenge, Relish is cleaved to generate two fragments, the DNA-binding transcription factor REL-68 and the I kappa B-like REL-49. Using transgenic fly strains we show here that overexpression of REL-68 separately from REL-49 is sufficient to activate strong constitutive transcription of the Diptericin gene, but little constitutive or inducible transcription of Attacin and Cecropin, two other Relish target genes. Their transcription may therefore require additional modifications of Relish. However, phosphorylation of the conserved serine residue S431 is not involved in such modifications. This is unlike p65 and Dorsal, which are modulated by phosphorylation at their homologous site. In contrast to other I kappa B proteins, overexpression of REL-49 had no inhibitory effect on Relish-dependent transcription. Instead, we propose that the C-terminal I kappa B-like domain executes a scaffolding and recruiting function for full activation of Relish.

Place, publisher, year, edition, pages
2009. Vol. 33, no 5, 690-696 p.
Keyword [en]
Innate immune response, Rel homology domain, I kappa B-like, Phosphorylation, Caspase cleavage, Scaffolding, Compound Rel protein, Antimicrobial peptide gene
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-60254DOI: 10.1016/j.dci.2008.12.002ISI: 000264001200006OAI: diva2:433999
authorCount :5Available from: 2011-08-12 Created: 2011-08-11 Last updated: 2011-08-12Bibliographically approved

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