A comparison between homologous and heterologous RNA polymerase recognition sites during in vitro chromatin transcription.

Abstract

To analyze the in vitro specificity of homologous and heterologous transcription systems, the template specificities of pea and cauliflower RNA polymerase II for pea chromatin were studied and compared with the specificity exhibited by the Escherichia coli holoenzyme. The results with pea chromatin show that the two eukaryotic enzymes compete with each other for the same recognition sites, but the E. coli enzyme utilizes different recognition sites. The data indicate that during transcription of chromatin in vitro, heterologous eukaryotic RNA polymerase II recognizes the same sites as the homologous enzyme, but the E. coli enzyme does not c enzymes compete with each other for the same recognition sites, but the E. coli enzyme utilizes different recognition sites. The data indicate that during transcription of chromatin in vitro, heterologous eukaryotic RNA polymerase II recognizes the same sites as the homologous enzyme, but the E. coli enzyme does not c enzymes compete with each other for the same recognition sites, but the E. coli enzyme utilizes different recognition sites. The data indicate that during transcription of chromatin in vitro, heterologous eukaryotic RNA polymerase II recognizes the same sites as the homologous enzyme, but the E. coli enzyme does not recognize these sites. In contrast to the situation with chromatin, all three enzymes utilize the same recognition sites on DNA. These results suggest the presence of proteins in chromatin which specifically interact with eukaryotic RNA polymerase II but not with the bacterial enzyme, or a possible template structure in chromatin which can be recognized by eukaryotic enzyme but not by E. coli enzyme.