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DNA-dependent RNA polymerase from Halobacterium halobium.

W Zillig·K O Stetter·M Tobien
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Abstract

DNA-dependent RNA polymerase core enzyme was isolated from Halobacterium halobium. The purification is based on the finding that the enzyme is stable in 40% (v/v) glycerol, in the presence of 0.05 M MgCl2 and involves adsorption of contaminants to DEAE-cellulose, precipitation of the complex of polymerase with DNA by streptomycin sulfate, chromatography over Biogel and affinity chromatography over heparin-Sepharose or heparin-cellulose. The enzyme consists of four or five different subunits. The composition formula was estimated as (150000) (86000)2 (72000)2 (49000)3 or 2; there may be one or two different 49000-Mr subunits. RNA synthesis requires a template. Denatured DNA is more efficient than native DNA. The transcription of native DNA is specifically stimulated by the addition of a possibly sigma-like factor eluted from DEAE-cellulose. The fidelity of transcription is indicated by the absolute requirement for UTP besides ATP with poly[d(A-T)] as the template.

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DNA-Directed RNA PolymerasesHalobacteriumKineticsMacromolecular SubstancesMolecular WeightTemplates, GeneticTranscription, GeneticJournal Article

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BibTeXRIS

W Zillig, K O Stetter, M Tobien. 1978-11-02. DNA-dependent RNA polymerase from Halobacterium halobium.. https://doi.org/10.1111/j.1432-1033.1978.tb20951.x

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