Molecular cloning and characterization of SRAM, a novel insect rel/ankyrin-family protein present in nuclei.
Molecular cloning and characterization of SRAM, a novel insect rel/ankyrin-family protein present in nuclei.
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SRAM 的分子克隆和表征,SRAM 是一种存在于细胞核中的新型昆虫 rel/锚蛋白家族蛋白。
DOI:
10.1093/oxfordjournals.jbchem.a022708
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发表时间:
2000
影响因子:
2.7
通讯作者:
S. Natori
中科院分区:
文献类型:
--
作者:
H. Shiraishi;A. Kobayashi;Y. Sakamoto;T. Nonaka;Y. Mitsui;N. Aozasa;T. Kubo;S. Natori
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.