Wg. Gu et D. Reines, IDENTIFICATION OF A DECAY IN TRANSCRIPTION POTENTIAL THAT RESULTS IN ELONGATION-FACTOR DEPENDENCE OF RNA-POLYMERASE-II, The Journal of biological chemistry, 270(19), 1995, pp. 11238-11244
The rate of RNA elongation by RNA polymerase II (pol II) is affected b
y DNA sequences called intrinsic arrest sites. Efficient transcription
through these sites requires elongation factor SII. In addition to th
e sequence-specific features of the DNA, we show that the acquisition
of SII-dependence is a function of its ''dwell-time'' at an arrest sit
e. This temperature-dependent decay in elongation potential appears ir
reversible, implying that factor-dependent and factor-independent elon
gation complexes are not mutually interconvertible at this position. T
FIIF and NH4Cl are known to increase the elongation rate of pol II. Bo
th agents preempt arrest, consistent with the idea that elongation dwe
ll time influences the process. TFIIF and SII act upon different steps
in a complementary way to prevent or resolve arrest, respectively. Th
ey are probably instrumental in facilitating the efficient transcripti
on of large eukaryotic genes in vivo.