Abstract
The rate of RNA elongation by RNA polymerase II (pol II) is affected by DNA sequences called intrinsic arrest sites. Efficient transcription through these sites requires elongation factor SII. In addition to the sequence-specific features of the DNA, we show that the acquisition of SII-dependence is a function of its "dwell-time" at an arrest site. This temperature-dependent decay in elongation potential appears irreversible, implying that factor-dependent and factor-independent elongation complexes are not mutually interconvertible at this position. TFIIF and NH4Cl are known to increase the elongation rate of pol II. Both agents preempt arrest, consistent with the idea that elongation dwell time influences the process. TFIIF and SII act upon different steps in a complementary way to prevent or resolve arrest, respectively. They are probably instrumental in facilitating the efficient transcription of large eukaryotic genes in vivo.