Abstract
An improved purification procedure is described for the rho transcription termination factor of Escherichia coli. The method involves lysozyme--sodium deoxycholate lysis, Polymin P fractionation, and chromatography on phosphocellulose, poly(uridylic acid)--Sepharose, and AMP--agarose. The method yields up to 9 mg of electrophoretically pure protein from 200 200 g of E. coli MRE 600. From quantitative amino acid analysis rho is calculated to have an E280nm (1%) of 3.7 +/- 0.3. The purified rho has an ATPase specific activity of 32 nmol of Pi released min-1 microgram-1 when poly(cytidylic acid) is used as a cofactor, and it functions effectively in termination of T7 DNA transcription. A subunit molecular weight of 48 000 for rho was determined by phosphate-buffered sodium dodecyl sulfate--polyacrylamide gel electrophoresis. The amino acid composition and circular dichroism spectrum in the far-ultraviolet for rho are presented.
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