Nucleic Acids Research, Vol 24, Issue 7 1238-1245, Copyright © 1996 by Oxford University Press
I Gross, P Georgel, C Kappler, JM Reichhart and JA Hoffmann
In Drosophila, bacterial challenge induces the rapid transcription of
several genes encoding potent antibacterial peptides. The upstream
sequences of the diptericin and cecropin Al genes, which have been
investigated in detail, contain two, respectively one sequence element
homologous to the binding site of the mammalian nuclear factor kappaB.
These elements have been shown to be mandatory for immune-induced
transcription of both genes. Functional studies have shown that these
kappaB-related elements can be the target for the Drosophila Rel proteins
dorsal and Dif. Here we present a comparative analysis of the
transactivating capacities of these proteins on reporter genes fused to
either the diptericin or the cecropin kappaB-related motifs. We conclude
from our results: (i) the kappaB motifs of the diptericin and cecropin
genes are not functionally equivalent; (ii) the dorsal and Dif proteins
have distinct DNA-binding characteristics; (iii) dorsal and Dif can
heterodimerize in vitro; (iv) mutants containing no copies of dorsal and a
single copy of Dif retain their full capacity to express the diptericin and
cecropin genes in response to challenge.
ARTICLES
Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin
Institut de Biologie Moleculaire et Cellulaire, CNRS, Strasbourg, France.
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