Sukhodolets M V, Jin D J
Laboratory of Molecular Biology, NCI, National Institutes of Health, Bethesda, MD 20892, USA.
J Biol Chem. 1998 Mar 20;273(12):7018-23. doi: 10.1074/jbc.273.12.7018.
We have identified a novel Escherichia coli RNA polymerase (RNAP)-associated protein, an ATPase named RapA. Almost all of this 110-kDa protein in the cell copurifies with RNAP holoenzyme as a 1:1 complex. Purified to homogeneity, RapA also forms a stable complex with RNAP, as if it were a subunit of RNAP. The ATPase activity of RapA is stimulated by binding to RNAP, and thus, RapA and RNAP interact physically as well as functionally. Interestingly, RapA is a homolog of the SWI/SNF family of eukaryotic proteins whose members are involved in transcription activation, nucleosome remodeling, and DNA repair.
我们鉴定出一种新型的大肠杆菌RNA聚合酶(RNAP)相关蛋白,一种名为RapA的ATP酶。细胞中几乎所有这种110 kDa的蛋白都与RNAP全酶以1:1复合物的形式共同纯化。纯化至同质后,RapA也与RNAP形成稳定的复合物,就好像它是RNAP的一个亚基一样。RapA的ATP酶活性通过与RNAP结合而被刺激,因此,RapA与RNAP在物理和功能上都相互作用。有趣的是,RapA是真核蛋白SWI/SNF家族的同源物,该家族成员参与转录激活、核小体重塑和DNA修复。