Kikukawa Yuhsuke, Shimada Masumi, Suzuki Norio, Tanaka Keiji, Yokosawa Hideyoshi, Kawahara Hiroyuki
Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Biol Chem. 2002 Jul-Aug;383(7-8):1257-61. doi: 10.1515/BC.2002.139.
Recognition of polyubiquitinated substrates by the 26S proteasome is a key step in the selective degradation of various cellular proteins. The Rpn10 subunit of the 26S proteasome can bind polyubiquitin conjugates in vitro. We have previously reported the unique diversity of Rpn10, which differs from other multiple proteasome subunits, and that the mouse Rpn10 mRNA family is generated from a single gene by developmentally regulated alternative splicing. To determine whether such alternative splicing mechanisms occur in other species, we searched for Rpn10 isoforms in databases and in our original PCR products. Here we report the genomic organization of the Rpn10 gene in lower vertebrates and provide evidence for the competent generation of distinct forms of Rpn10 by alternative splicing through evolution.
26S蛋白酶体识别多聚泛素化底物是各种细胞蛋白质选择性降解的关键步骤。26S蛋白酶体的Rpn10亚基在体外可结合多聚泛素缀合物。我们之前报道过Rpn10独特的多样性,它不同于其他多个蛋白酶体亚基,并且小鼠Rpn10 mRNA家族是由一个单一基因通过发育调控的可变剪接产生的。为了确定这种可变剪接机制是否在其他物种中发生,我们在数据库和我们最初的PCR产物中搜索Rpn10异构体。在此我们报道了低等脊椎动物中Rpn10基因的基因组结构,并提供证据表明通过进化可变剪接能够产生不同形式的Rpn10。