Abstract:
:A new procedure for the purification of B. subtilis RNA polymerase, based on mild lysis of cells, low speed centrifugation, gel filtration, DEAE-Sephadex chromatography and affinity chromatography on DNA-cellulose, yields three forms of enzyme referred here as enzyme A, B and C. As revealed by SDS gel electrophoresis, enzyme A has 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 beta factor. Enzyme C has the holo-enzyme composition. The pattern of sensitivity of the three forms of enzyme towards KCl are very different: enzymes A and B, even at low concentration of 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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Plevan P,Albertini AM,Galizzi A,Adamoli A,Mastromei G,Riva S,Cassani Gdoi
10.1093/nar/4.3.603subject
Has Abstractpub_date
1977-03-01 00:00:00pages
603-23issue
3eissn
0305-1048issn
1362-4962journal_volume
4pub_type
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