A protein–protein interaction map of yeast RNA polymerase III
Copyright policy )A protein–protein interaction map of yeast RNA polymerase III
The structure of the yeast RNA polymerase (pol) III was investigated by exhaustive two-hybrid screening using a library of random genomic fragments fused to the Gal4 activation domain. This procedure allowed us to identify contacts between individual polypeptides, localize the contact domains, and deduce a protein–protein interaction map of the multisubunit enzyme. In all but one case, pol III subunits were able to interactin vivowith one or sometimes two partner subunits of the enzyme or with subunits of TFIIIC. Four subunits that are common to pol I, II, and III (ABC27, ABC14.5, ABC10α, and ABC10β), two that are common to pol I and III (AC40 and AC19), and one pol III-specific subunit (C11) can associate with defined regions of the two large subunits. These regions overlapped with highly conserved domains. C53, a pol III-specific subunit, interacted with a 37-kDa polypeptide that copurifies with the enzyme and therefore appears to be a unique pol III subunit (C37). Together with parallel interaction studies based on dosage-dependent suppression of conditional mutants, our data suggest a model of the pol III preinitiation complex.
Binding Sites, Transcription, Genetic, Macromolecular Substances, Recombinant Fusion Proteins, RNA Polymerase III, Saccharomyces cerevisiae, Open Reading Frames, Peptide Library, RNA Polymerase I, Transcription Factors, TFIII, Transcription Factor TFIIIC, RNA Polymerase II, Conserved Sequence, Transcription Factors
Binding Sites, Transcription, Genetic, Macromolecular Substances, Recombinant Fusion Proteins, RNA Polymerase III, Saccharomyces cerevisiae, Open Reading Frames, Peptide Library, RNA Polymerase I, Transcription Factors, TFIII, Transcription Factor TFIIIC, RNA Polymerase II, Conserved Sequence, Transcription Factors
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