Open AccessRNA Polymerases of Maize: Nuclear RNA Polymerases
Author(s) -
Gustave C. Strain,
Kathleen P. Mullinix,
Lawrence Bogorad
Publication year - 1971
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.68.11.2647
Subject(s) - enzyme , polymerase , dna , biochemistry , rna , dna polymerase , biology , rna polymerase , microbiology and biotechnology , chemistry , gene
Two DNA-dependent RNA polymerases of nuclear origin have been purified from leaves ofZea mays . The two enzymes can be separated on DEAE-cellulose columns. Enzymes I and II are eluted with 0.08 and 0.20 M (NH4 )2 SO4 , respectively. Both enzymes prefer maize nuclear DNA as a template; they are also more active in the presence of Mg++ than Mn++ and are inhibited by (NH4 )2 -SO4 or KCl. Neither enzyme is inhibited by rifamycin SV. Enzyme II is strongly inhibited by α-amanitin, whereas enzyme I is not significantly affected. Their ability to use native and denatured DNA as templates varies according to the extent and method of purification of the polymerase. Furthermore, enzyme II can be resolved by DEAE-chromatography or glycerol-gradient centrifugation into two components, one of which prefers native DNA, while the other prefers denatured DNA.