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Vol. 12, No. 3, pp. 343-356, February 1, 1998
1 Faculty of Bioscience and Biotechnology, Tokyo
Institute of Technology, Midori-ku, Yokohama 226, Japan;
2 National Institute of Genetics, Mishima, Shizuoka-ken 411, Japan;
3 Tokyo Research Laboratories, Kyowa Hakko Kogyo Co.,
Ltd., Machida-shi 194, Japan;
4 Department of Genetics and
5 Department of Biological Chemistry and Molecular
Pharmacology, Harvard Medical School,
Boston, Massachusetts 02115 USA
We report the identification of a transcription elongation factor
from HeLa cell nuclear extracts that causes pausing of RNA polymerase
II (Pol II) in conjunction with the transcription inhibitor 5,6-dichloro-1-
-D-ribofuranosylbenzimidazole (DRB). This
factor, termed DRB
sensitivity-inducing factor
(DSIF), is also required for transcription inhibition by H8. DSIF has
been purified and is composed of 160-kD (p160) and 14-kD (p14)
subunits. Isolation of a cDNA encoding DSIF p160 shows it to be a
homolog of the Saccharomyces cerevisiae transcription factor
Spt5. Recombinant Supt4h protein, the human homolog of yeast Spt4, is
functionally equivalent to DSIF p14, indicating that DSIF is composed
of the human homologs of Spt4 and Spt5. In addition to its negative
role in elongation, DSIF is able to stimulate the rate of elongation by
RNA Pol II in a reaction containing limiting concentrations of
ribonucleoside triphosphates. A role for DSIF in transcription
elongation is further supported by the fact that p160 has a region
homologous to the bacterial elongation factor NusG. The combination of
biochemical studies on DSIF and genetic analysis of Spt4 and Spt5 in
yeast, also in this issue, indicates that DSIF associates with RNA Pol II and regulates its processivity in vitro and in vivo.
[Key Words: DRB; DSIF; transcription elongation; transcription elongation factor; transcription inhibitor; protein phosphorylation; NusG]
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