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J Biol Chem, Vol. 273, Issue 12, 7018-7023, March 20, 1998

RapA, a Novel RNA Polymerase-Associated Protein, Is a Bacterial Homolog of SWI2/SNF2

Maxim V. Sukhodolets and Ding Jun Jin

From the Laboratory of Molecular Biology, NCI, National Institutes of Health, Bethesda, MD 20892

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.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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