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J. Biol. Chem., Vol. 262, Issue 30, 14377-14380, Oct, 1987
M Riva, AR Schaffner, A Sentenac, GR Hartmann, AA Mustaev, EF Zaychikov and MA Grachev
RNA polymerases A, B, and C from yeast were modified by reaction with 4-
formylphenyl-gamma-ester of ATP as priming nucleotide followed by reduction
with NaBH4. Upon phosphodiester bond formation with [alpha- 32P]UTP, only
the second largest subunit, A135, B150, or C128, was labeled in a
template-dependent reaction. This indicates that these polypeptide chains
are functionally homologous. The product covalently bound to B150 subunit
was found to consist of a mixture of ApU and a trinucleotide. Enzyme
labeling exhibited the characteristic alpha- amanitin sensitivity reported
for A and B RNA polymerases. Labeling of both large subunits of enzyme A
and B but not of any of the smaller subunits was observed when the
reduction step stabilizing the binding of the priming nucleotide was
carried out after limited chain elongation. These results illustrate the
conservative evolution of the active site of eukaryotic RNA polymerases.
Active site labeling of the RNA polymerases A, B, and C from yeast
Service de Biochimie, Centre d'Etudes Nucleaires de Saclay, Gif-sur- Yvette, France.
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