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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Molecular cloning and characterization of SRAM, a novel insect rel/ankyrin-family protein present in nuclei.

Previously, we purified a 59-kDa protein that binds to the kappaB motif of the Sarcophaga lectin gene. Here we report its cDNA cloning and some of its characteristics as a novel member of the Rel/Ankyrin-family. This protein, named SRAM, contained a Rel homology domain, a nuclear localization signal and 4 ankyrin repeats, but lacked the Ser-rich domain and PEST sequence that Relish 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 lectin gene promoter containing tandem repeats of the kappaB motifs was activated in NIH-Sape-4 cells. In Drosophila mbn-2 cells, Dif alone activated this reporter gene and a cooperative effect was detected when SRAM and Dif were co-transfected, although SRAM alone did not activate it. This is the first report of a Rel/Ankyrin molecule that exists in the nuclei.[1]

References

  1. Molecular cloning and characterization of SRAM, a novel insect rel/ankyrin-family protein present in nuclei. Shiraishi, H., Kobayashi, A., Sakamoto, Y., Nonaka, T., Mitsui, Y., Aozasa, N., Kubo, T., Natori, S. J. Biochem. (2000) [Pubmed]
 
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