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. 1975 Aug;72(8):3034–3038. doi: 10.1073/pnas.72.8.3034

Dissociation of two polypeptide chains from yeast RNA polymerase A.

J Huet, J M Buhler, A Sentenac, P Fromageot
PMCID: PMC432913  PMID: 1103135

Abstract

Yeast RNA polymerase A (RNA nucleotidyltransferase; nucleosidetriphosphate:RNA nucleotidyltransferase; EC 2.7.7.6) can be converted to a new form of enzyme, called RNA polymerase A*, which is lacking two polypeptide chains of 48,000 and 37,000 daltons. Apart from these two missing polypeptides the subunit structures of RNA polymerases A and A* are indistinguishable. RNA polymerase A* differs from the complete enzyme in its electrophoretic and chromatographic behavior, template requirements, and alpha-amanitin sensitivity. RNA polymerase A* transcribes the alternated copolymer d(A-T)n with the same efficiency as RNA polymerase A but its specific activity is greatly reduced with native calf thymus DNA as template. The transcription of a variety of synthetic templates is also altered by removal of the two polypeptide chains. RNA polymerase A* is inhibited by high concentrations of alpha-amanitin (500 mug/ml), whereas RNA polymerase A is comparatively less sensitive to the toxic peptide. The data are discussed in terms of possible roles of the two dissociable polypeptides.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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