Aravind L, Ponting C P
Department of Biology-BSBW, Texas A&M University, College Station 77843, USA.
Protein Sci. 1998 May;7(5):1250-4. doi: 10.1002/pro.5560070521.
Single copies of an alpha-helical-rich motif are demonstrated to be present within subunits of the large multiprotein 26S proteasome and eukaryotic initiation factor-3 (eIF3) complexes, and within proteins involved in transcriptional regulation. In addition, p40 and p47 subunits of eIF3 are shown to be homologues of the proteasome subunit Mov34, and transcriptional regulators JAB1/pad1. Finally, the proteasome subunit S5a and the p44 subunit of the basal transcription factor IIH (TFIIH) are identified as homologues. The presence of homologous, and sometimes identical, proteins in contrasting functional contexts suggests that the large multisubunit complexes of the 26S proteasome, eIF3 and TFIIH perform overlapping cellular roles.
富含α-螺旋的基序的单拷贝被证明存在于大型多蛋白26S蛋白酶体和真核起始因子-3(eIF3)复合物的亚基中,以及参与转录调控的蛋白质中。此外,eIF3的p40和p47亚基被证明是蛋白酶体亚基Mov34和转录调节因子JAB1/pad1的同源物。最后,蛋白酶体亚基S5a和基础转录因子IIH(TFIIH)的p44亚基被鉴定为同源物。在不同功能背景下存在同源甚至有时相同的蛋白质,这表明26S蛋白酶体、eIF3和TFIIH的大型多亚基复合物在细胞中发挥重叠的作用。