PRE5 AND PRE6, THE LAST MISSING GENES ENCODING 20S PROTEASOME SUBUNITS FROM YEAST - INDICATION FOR A SET OF 14 DIFFERENT SUBUNITS IN THE EUKARYOTIC PROTEASOME CORE
PRE5 AND PRE6, THE LAST MISSING GENES ENCODING 20S PROTEASOME SUBUNITS FROM YEAST - INDICATION FOR A SET OF 14 DIFFERENT SUBUNITS IN THE EUKARYOTIC PROTEASOME CORE
复制标题
DOI：
10.1021/bi00206a028
复制
发表时间：
1994-10-11
期刊：
影响因子：
2.9
通讯作者：
WOLF, DH
中科院分区：
文献类型：
--
作者：
HEINEMEYER, W;TRONDLE, N;WOLF, DH
真核生物的20 S蛋白酶体是一种丰富的多催化/多功能蛋白酶复合物，由蛋白酶体基因家族的α或β型成员编码的一系列不同亚基组成。目前，在芽殖酵母中已检测到14个亚基，并克隆了12个蛋白酶体基因。从酵母20 S蛋白酶体的纯化亚基的肽序列开始，我们克隆了两个额外的prc，teasomal基因，PRE 5和PRE 6，它们都编码必需的α-型亚基。所有已知的真核生物蛋白酶体蛋白的序列比较显示存在总共14个亚组，其可分为7个α-和7个β-型组。包括Pre 5和Pre 6蛋白质，每个亚组包含单个酵母成员。我们预计，14个基因编码亚基的酵母蛋白酶体代表了完整的蛋白酶体基因的这种生物体。古细菌蛋白酶体的祖先是由四个堆叠的环组成，两个外环含有七个相同的a-亚基，内环含有七个相同的β-亚基。我们推测，与古细菌蛋白酶体类似，每个真核生物蛋白酶体由14个不同亚基的两半组成，每一半由7个不同的α型和7个不同的β型亚基组成。在高等真核生物中，亚基亚型可能有助于20 S蛋白酶体的亚基组成的变异性，从而允许功能调节。
The 20S proteasome of eukaryotes is an abundant multicatalytic/multifunctional proteinase complex composed of an array of nonidentical subunits which are encoded by alpha- or beta-type members of the proteasomal gene family. In budding yeast, 14 subunits had been detected and 12 proteasomal genes had been cloned and sequenced so far. Starting from peptide sequences of purified subunits of the yeast 20S proteasome, we cloned two additional prc,teasomal genes, PRE5 and PRE6, which both encode essential alpha-type subunits. Sequence comparison of al known eukaryotic proteasomal proteins show the presence of a total of 14 subgroups, which can be divided into seven alpha- and seven beta-type groups. Including the Pre5 and Pre6 proteins, every subgroup contains a single yeast member. We anticipate that the 14 genes encoding subunits of the yeast proteasome represent the complete set of proteasomal genes of this organism. The ancestral archaebacterial proteasome is composed of four stacks of rings, the two outer rings containing seven identical a-subunits and the inner rings containing seven identical beta-subunits. We speculate that, in analogy to the archaebacterial proteasome, every eukaryotic proteasome is made of two halves of 14 distinct subunits, each half consisting of seven different alpha-type and 7 different beta-type subunits. In higher eukaryotes, subunit isoforms may contribute to variability in the subunit composition of the 20S proteasome allowing functional modulations.