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Molecular Organization of the 20S Proteasome Gene Family from Arabidopsis thaliana

机译:拟南芥20S蛋白酶体基因家族的分子组织

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The 20S proteasome is the proteolytic complex in eukaryotes responsible for degrading short-lived and abnormal intracellular proteins, especially those targeted by ubiquitin conjugation. The 700-kD complex exists as a hollow cylinder comprising four stacked rings with the catalytic sites located in the lumen. The two outer rings and the two inner rings are composed of seven different α and β polypeptides, respectively, giving an α7/β7/β7/α7 symmetric organization. Here we describe the molecular organization of the 20S proteasome from the plant Arabidopsis thaliana. From an analysis of a collection of cDNA and genomic clones, we identified a superfamily of 23 genes encoding all 14 of the Arabidopsis proteasome subunits, designated PAA-PAG and PBA-PBG for P roteasome A lpha and B eta subunits A–G , respectively. Four of the subunits likely are encoded by single genes, and the remaining subunits are encoded by families of at least 2 genes. Expression of the α and β subunit genes appears to be coordinately regulated. Three of the nine Arabidopsis proteasome subunit genes tested, PAC1 (α3), PAE1 (α5) and PBC2 (β3), could functionally replace their yeast orthologs, providing the first evidence for cross-species complementation of 20S subunit genes. Taken together, these results demonstrate that the 20S proteasome is structurally and functionally conserved among eukaryotes and suggest that the subunit arrangement of the Arabidopsis 20S proteasome is similar if not identical to that recently determined for the yeast complex.
机译:20S蛋白酶体是真核生物中的蛋白水解复合物,负责降解短命和异常的细胞内蛋白质,特别是泛素结合靶向的蛋白质。 700-kD络合物是一个空心圆柱体,包含四个堆叠的环,催化位点位于内腔中。两个外环和两个内环分别由七个不同的α和β多肽组成,形成α7/β7/β7/α7对称组织。在这里,我们描述了植物拟南芥中20S蛋白酶体的分子组织。通过对一系列cDNA和基因组克隆的分析,我们确定了23个基因的超家族,该基因编码拟南芥蛋白酶体的所有14个亚基,分别命名为P蛋白酶体A lpha和B eta A-G的PAA-PAG和PBA-PBG。 。四个亚基可能由单个基因编码,而其余的亚基则由至少2个基因的家族编码。 α和β亚基基因的表达似乎受到协调调节。测试的九个拟南芥蛋白酶体亚基基因中的三个,PAC1(α3),PAE1(α5)和PBC2(β3),可以在功能上替代其酵母直系同源基因,为20S亚基基因的跨物种互补提供了第一个证据。综上所述,这些结果表明20S蛋白酶体在真核生物中在结构和功能上是保守的,并且表明拟南芥20S蛋白酶体的亚基排列与最近针对酵母复合物确定的亚基排列相似或相似。

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