Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease
Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease
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DOI：
10.1016/0014-5793(96)00101-9
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发表时间：
1996-02-26
期刊：
影响因子：
3.5
通讯作者：
Rechsteiner, M
中科院分区：
文献类型：
--
作者：
Ferrell, K;Deveraux, Q;Rechsteiner, M
S5a是26S蛋白酶的一个亚基，它结合并可能选择多泛素化蛋白进行破坏。我们最近发现了一种拟南芥蛋白MBP1，它在物理上、免疫学上和生化上与人红细胞26S蛋白酶的S5a相似。基于MBP1 cDNA序列，我们现在已经分离出了一个编码人类S5a的HeLa细胞cDNA。HeLa cDNA序列与MBP1高度相似，它编码直接从人红细胞S5a中获得的肽。此外，将分离的cDNA在大肠杆菌中表达得到的重组蛋白具有明显的分子质量和多泛素结合特性，与纯化的26S酶获得的人S5a相匹配。
S5a is a subunit of the 26S protease that binds and presumably selects multiubiquitinated proteins for destruction, We recently identified an Arabidopsis protein, MBP1, that is physically, inmunologically and biochemically similar to S5a from the human erythrocyte 26S protease. Based upon the MBP1 cDNA sequence we have now isolated a HeLa cell cDNA coding for human S5a. The HeLa cDNA sequence is highly similar to MBP1 and it encodes peptides obtained directly from human erythrocyte S5a. Moreover, expression of the isolated cDNA in E. coli results in a recombinant protein with an apparent molecular mass and multiubiquitin binding properties that match those of human S5a obtained from the purified 26S enzyme.