H. Shiraishi et al., Molecular cloning and characterization of SRAM, a novel insect Rel/Ankyrin-family protein present in nuclei, J BIOCHEM, 127(6), 2000, pp. 1127-1134
Previously, we purified a 59-kDa protein that binds to the KB motif of the
Sarcophaga lectin gene. Here we report its cDNA cloning and some of its cha
racteristics as a novel member of the Rel/Ankyrin-family. This protein, nam
ed SRAM, contained a Rel homology domain, a nuclear localization signal and
4 ankyrin repeats, but lacked the Ser-rich domain and PEST sequence that R
elish contained, We found that SRAM was localized in the nuclei of NIH-Sape
-4 cells, which are an embryonic cell line of Sarcophaga, The Sarcophaga le
ctin gene promoter containing tandem repeats of the kappa B moths was activ
ated in NIH-Sape-4 cells. In Drosophila mbn-2 cells, Dif alone activated th
is reporter gene and a cooperative effect was detected when SRAM and Dif we
re co-transfected, although SRAM alone did not activate it. This is the fir
st report of a Rel/Ankyrin molecule that exists in the nuclei.