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Papers In Press, published online ahead of print May 2, 2000
J. Biol. Chem, 10.1074/jbc.M000056200
Submitted on January 3, 2000
Accepted on May 2, 2000

Interaction between RNA polymerase and RapA, a bacterial homolog of the SWI/SNF protein family

Maxim V. Sukhodolets and Ding Jun Jin

Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892-4255

Corresponding Author: djjin{at}helix.nih.gov

Recently we identified a novel E. coli RNA polymerase(RNAP)-associated protein, an ATPase, called RapA (Sukhodolets & Jin, 1998, JBC, 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 et al., 1998, JBC, 273:15157-15161), our in vivo analysis of a rapA null mutant suggested that RapA is unlikely directly to be involved in DNA repair.


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