Purified yeast RNA polymerase II reads through intrinsic blocks to elongation in response to the yeast TFIIS analogue, P37.

摘要: Saccharomyces cerevisiae has a TFIIS-related transcription elongation factor, originally called P37 (Sawadogo, M., Sentenac, A., and Fromageot, P. (1979) J. Biol. Chem. 255, 12-15; Nakanishi, T., Nakano, Nomura, K., Sekimizu, Natori, S. (1992) 267, 13200-13204), which binds directly to RNA polymerase II stimulates read-through of intrinsic blocks elongation. To elucidate functional features this protein:protein interaction, we tested the ability several forms respond either full-length or an amino-terminal truncation TFIIS. The variants differed in structure carboxyl-terminal domain largest subunit lacked two smaller subunits. No differences recognize read through them response form TFIIS were detected among these variants. Furthermore, ternary complexes containing each variant cleave 3' end nascent transcripts TFIIS, reaction previously reported for mammalian Drosophila (Kassavetis, G. Geiduschek, E. (1993) Science 259, 944-945) likely be important function. Thus subunits four seven polymerase, required vivo, are not vitro recognition elongation, TFIIS-stimulated cleavage transcript.