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Nucleic Acids Research, 1977, Vol. 4, No. 3 603-623
© 1977

Articles

RNA polymerase from Bacillus subtilis: isolation of core and holo enzyme by DNA-cellulose chromatography

Paolo Plevani1, Alessandra M. AIbertini2, Alessandro Galizzi2, Anna Adamoli1, Giorgio Mastromei2, Silvano Riva2 and Giovanni Cassani3

1Ente Universitario Lombardia Orientale Corsi di Medicina, Brescia 2Istituto di Genetica dell' Università e Laboratorio di Genetica Biochimica ed Evoluzionistica del CNR Pavia 3Istituto di Biologia Generale dell'Università di Milano Italy

Received December 16, 1976. A new procedure for the purification of B. subtilis RNA polymerase, based on mild lysis of cells, low speed centrifugation, gelfiltration, DEAE-Sephadex chromatography and affinity chromatography on DNA-cel-lulose, yields three forms of enzyme referred here as enzyme A, B and C. As revealed by SDS gel electrophoresis, enzyme Ahas the subunit structure of core polymerase plus some small polypeptides. Its catalytic properties are similar to those of core polymerase. Enzyme B has the composition of core polymerase. Both enzymes A and B can be stimulated by the addition of 6 factor. Enzyme C has the holo-enzyme composition. The pattern of sensitivity of the three forms of enzyme towards KC1 are very different: enzymes A and B, even at low concentrationof salt, are inhibited with all the DNA templates tested, whereas enzyme C shows a pattern of stimulation specific for each DNA tested. The transcripts of the three enzymes on phage SPP1 DNA template have been analyzed by hybridization to the separated strands. Only enzyme C selectively transcribed the H strands.


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