Similar subunit architecture of archaeal and eukaryal RNA polymerases

被引:12
作者
Best, AA [1 ]
Olsen, GJ [1 ]
机构
[1] Univ Illinois, Dept Microbiol, Chem & Life Sci Lab B103, Urbana, IL 61801 USA
关键词
affinity pulldown; archaeon; protein interaction; RNA polymerase; transcription;
D O I
10.1016/S0378-1097(00)00550-4
中图分类号
Q93 [微生物学];
学科分类号
071005 [微生物学]; 100705 [微生物与生化药学];
摘要
Protein interactions among RNA polymerase small subunits from the archaeon Methanococcus jannaschii were investigated using affinity pulldown assays in pairwise and higher-order combinations. In the most extensive study of archaeal RNA polymerase subunit interactions to dare. including 37 pairs of proteins. 10 ternary combinations, and three quaternary combinations, we found evidence for pairwise interactions of subunit D with subunits L and N. and a ternary complex of subunits D, L and N. No other small subunit interactions occurred. These results are consistent with interactions observed in a crystal structure of eukaryotic RNA polymerase II and support a common archaeal/eukaryal RNA polymerase architecture. We further propose that subunit E-n is not an integral member of archaeal RNA polymerases. Finally, we discuss the relative accuracy of the various methods that have been used to predict protein-protein interactions in RNA polymerase. (C) 2001 Federation of European Microbiological Societies, Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:85 / 90
页数:6
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