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PMID: 5288239 Published · ppublish English Journal Article

RNA polymerases of maize: nuclear RNA polymerases.

Strain GC, Mullinix KP, Bogorad L

Abstract

Two DNA-dependent RNA polymerases of nuclear origin have been purified from leaves of Zea mays. The two enzymes can be separated on DEAE-cellulose columns. Enzymes I and II are eluted with 0.08 and 0.20 M (NH(4))(2)SO(4), 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 (NH(4))(2)-SO(4) or KCl. Neither enzyme is inhibited by rifamycin SV. Enzyme II is strongly inhibited by alpha-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.

MeSH Terms
Ammonium Sulfate Centrifugation, Density Gradient Chromatography, DEAE-Cellulose DNA/isolation & purification Magnesium Manganese Potassium Chloride RNA Nucleotidyltransferases/antagonists & inhibitors,isolation & purification Rifampin Templates, Genetic Zea mays/enzymology
Chemicals
Manganese Potassium Chloride DNA RNA Nucleotidyltransferases Magnesium Ammonium Sulfate Rifampin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Strain G C
Mullinix K P
Bogorad L
References (12)
12 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1971-11-00
Pages
2647-51
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC389492
Subset
IM
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