Purification and Properties of RNA Polymerases from Mother Cells and Forespores of Sporulating Cells of Bacillus subtilis

Publisher Website
Google Scholar
Abstract
Bacillus subtilis sporulating cells at stage III were fractionated into mother cell and forespore fractions by means of a lysozyme-detergent method. Three forms of DNA-dependent RNA polymerase enzymes, termed Mσ, Fσ, and Fδ, in addition to core enzyme (α2,β′, and β) have been purified from the cell fractions. Enzymes Mσ and Fσ are present in the mother cell and forespore, respectively, and contain a factor of 55, 000 daltons in addition to the core subunits. On the other hand, enzyme Fδ is present specifically in the forespore and contains δ1 factor of 28, 000 daltons instead of the a factor. The amount of RNA polymerase in the forespore is about twice that in the mother cell. The enzymes Mσ and Fσ also differed in their elution profiles from DEAE-cellulose columns and in their heat stabilities indicating that the two σ-containing holoenzyme forms may be different in their structural properties. The enzyme Fδ transcribed B. subtilis DNA about 1.6 times more actively than enzyme Fσ, and the enzymes Mσ and Fσ transcribed the DNA about 2.2 times more actively than did core enzyme.

This publication has 2 references indexed in Scilit: