On the Phosphorylation of Yeast RNA Polymerases A and B

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Abstract

In exponentially growing cells, RNA polymerase B is exclusively form BI enzyme with several phosphorylated subunits: B220, B23 and possibly B44.5. In RNA polymerase A an average of fifteen phosphate groups are distributed on the five phosphorylated subunits: A190 (6), A43 (4), A34.5 (2), A23 (1—2) and A19 (1—2). Phosphorylation of enzyme A by a yeast protein kinase in vitro adds less than 1 mol phosphate/mol enzyme but occurs essentially at the physiological sites, as shown by a comparison of the peptide patterns obtained by limited proteolysis of subunits 32P‐labelled in vivo and in vitro. No evidence was found in favour of a modulation of RNA polymerase activity in vitro or in vivo via phosphorylation. Copyright © 1983, Wiley Blackwell. All rights reserved

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BRÉNT, B., BUHLER, J. ‐M, SENTENAC, A., & FROMAGEOT, P. (1983). On the Phosphorylation of Yeast RNA Polymerases A and B. European Journal of Biochemistry, 130(2), 247–251. https://doi.org/10.1111/j.1432-1033.1983.tb07143.x

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