Journal Article

Molecular Cloning and Characterization of SRAM, a Novel Insect Rel/Ankyrin-Family Protein Present in Nuclei

Hirohisa Shiraishi, Ayako Kobayashi, Yasumitsu Sakamoto, Takamasa Nonaka, Yukio Mitsui, Naohiko Aozasa, Takeo Kubo and Shunji Natori

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 127, issue 6, pages 1127-1134
Published in print June 2000 | ISSN: 0021-924X
Published online June 2000 | e-ISSN: 1756-2651 | DOI: https://dx.doi.org/10.1093/oxfordjournals.jbchem.a022708
Molecular Cloning and Characterization of SRAM, a Novel Insect Rel/Ankyrin-Family Protein Present in Nuclei

Show Summary Details

Preview

Previously, we purified a 59-kDa protein that binds to the κB 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 κB 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 SHAM and Dif were co-transfected, although SEAM alone did not activate it. This is the first report of a Rel/Ankyrin molecule that exists in the nuclei.

Keywords: ankyrin; insect immunity; κB motif; NF-κB/Rel family; Sarcophaga peregrina

Journal Article.  0 words. 

Subjects: Biochemistry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content. subscribe or login to access all content.