Activation mutants in yeast RNA polymerase II subunit RPB3 provide evidence for a structurally conserved surface required for activation in eukaryotes and bacteria

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Cold Spring Harbor Laboratory Press

RESUMO

We have identified a mutant in RPB3, the third-largest subunit of yeast RNA polymerase II, that is defective in activator-dependent transcription, but not defective in activator-independent, basal transcription. The mutant contains two amino-acid substitutions, C92R and A159G, that are both required for pronounced defects in activator-dependent transcription. Synthetic enhancement of phenotypes of C92R and A159G, and of several other pairs of substitutions, is consistent with a functional relationship between residues 92–95 and 159–161. Homology modeling of RPB3 on the basis of the crystallographic structure of αNTD indicates that residues 92–95 and 159–162 are likely to be adjacent within the structure of RPB3. In addition, homology modeling indicates that the location of residues 159–162 within RPB3 corresponds to the location of an activation target within αNTD (the target of activating region 2 of catabolite activator protein, an activation target involved in a protein–protein interaction that facilitates isomerization of the RNA polymerase promoter closed complex to the RNA polymerase promoter open complex). The apparent finding of a conserved surface required for activation in eukaryotes and bacteria raises the possibility of conserved mechanisms of activation in eukaryotes and bacteria.

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