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J. Biol. Chem., Vol. 275, Issue 29, 22090-22097, July 21, 2000

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Interaction between RNA Polymerase and RapA, a Bacterial Homolog of the SWI/SNF Protein Family^*

Maxim V. Sukhodolets and Ding Jun Jin

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

Recently, we identified a novel Escherichia coli RNA polymerase (RNAP)-associated protein, an ATPase, called RapA (Sukhodolets, M. V., and Jin, D. J. (1998) J. Biol. Chem. 273, 7018-7023). RapA is a bacterial homolog of SWI2/SNF2. We showed that RapA forms a stable complex with RNAP holoenzyme and that binding to RNAP holoenzyme stimulates the ATPase activity of RapA. We have further analyzed the interactions between purified RapA and the two forms of RNAP: core RNAP and RNAP holoenzyme. We found that RapA interacts with either form of RNAP. However, RapA exhibits higher affinity for core RNAP than for RNAP holoenzyme. Chemical cross-linking of the RNAP-RapA complex indicated that the RapA-binding sites are located at the interface between the  and ' subunits of RNAP. Contrary to previously reported results (Muzzin, O., Campbell, E., A., Xia, L., Severinova, E., Darst, S. A., and Severinov, K. (1998) J. Biol. Chem. 273, 15157-15161), our in vivo analysis of a rapA null mutant suggested that RapA is not likely to be directly involved in DNA repair.

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				B. A. McKinley and M. V. Sukhodolets Escherichia coli RNA polymerase-associated SWI/SNF protein RapA: evidence for RNA-directed binding and remodeling activity Nucleic Acids Res., December 18, 2007; 35(21): 7044 - 7060. [Abstract] [Full Text] [PDF]

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