van Riel M C, Martens G J
Department of Animal Physiology, University of Nijmegen, The Netherlands.
FEBS Lett. 1991 Oct 7;291(1):37-40. doi: 10.1016/0014-5793(91)81098-s.
The proteasome is a multicatalytic proteinase composed of a number of non-identical subunits. A Xenopus pituitary cDNA was isolated and found to code for the beta-subunit of proteasome. The amino acid sequence deduced from the open reading frame consisted of 215 amino acid residues with a calculated molecular weight of 23,979. A comparative structural analysis indicated that the proteasome subunits can be divided into two groups with the same evolutionary origin. One group consists of subunits with an N-terminally blocked residue and includes components C2, C3, C8 and C9, while the second group of non-blocked proteins includes component C5 and the beta-subunit.
蛋白酶体是一种由多个不同亚基组成的多催化蛋白酶。分离出一种非洲爪蟾垂体cDNA，发现其编码蛋白酶体的β亚基。从开放阅读框推导的氨基酸序列由215个氨基酸残基组成，计算分子量为23979。比较结构分析表明，蛋白酶体亚基可分为具有相同进化起源的两组。一组由N端残基封闭的亚基组成，包括组分C2、C3、C8和C9，而第二组非封闭蛋白包括组分C5和β亚基。
