RapA, a novel RNA polymerase-associated protein, is a bacterial homolog of SWI2/SNF2.
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.
Sukhodolets
M V
MV
Laboratory of Molecular Biology, NCI, National Institutes of Health, Bethesda, MD 20892, USA.
Jin
D J
DJ
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004926:Escherichia coli / Q000378:metabolism*; D009687:Nuclear Proteins; D014157:Transcription Factors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D014157:Transcription Factors; D012321:DNA-Directed RNA Polymerases; D000251:Adenosine Triphosphatases