TY - JOUR
T1 - Adriamycin inhibits human RH II/Gu RNA helicase activity by binding to its substrate
AU - Zhu, Kuichun
AU - Henning, Dale
AU - Iwakuma, Tomoo
AU - Valdez, Benigno C.
AU - Busch, Harris
N1 - Funding Information:
This work was supported by the Busch Fund. We thank Ms. R. K. Busch for technical support for our work. We also thank Drs. Ram Reddy and Pui K. Chan for reading the manuscript and providing valuable comments.
PY - 1999/12/20
Y1 - 1999/12/20
N2 - RNA helicases are enzymes important in RNA synthesis, processing, transport, and turnover. Human nucleolar RNA helicase II/Gu protein (RH II/Gu) was expressed in a baculovirus system. The purified recombinant RH II/Gu protein has RNA helicase activity on a 5' tailed ds RNA substrate in vitro. We found that Adriamycin, a widely used anticancer drug, inhibited RH II/Gu helicase activity in a dose-dependent manner with an IC50 of 40 μM. Adriamycin bound to the RNA substrate, and the binding was disrupted by boiling or treatment with 1% SDS, suggesting that the binding of Adriamycin to RNA is reversible. Adriamycin was also found by gel electrophoresis to bind to yeast tRNA to form slow-migrating complexes. These results suggest that Adriamycin can inhibit RNA synthesis or processing by binding to RNA substrates.
AB - RNA helicases are enzymes important in RNA synthesis, processing, transport, and turnover. Human nucleolar RNA helicase II/Gu protein (RH II/Gu) was expressed in a baculovirus system. The purified recombinant RH II/Gu protein has RNA helicase activity on a 5' tailed ds RNA substrate in vitro. We found that Adriamycin, a widely used anticancer drug, inhibited RH II/Gu helicase activity in a dose-dependent manner with an IC50 of 40 μM. Adriamycin bound to the RNA substrate, and the binding was disrupted by boiling or treatment with 1% SDS, suggesting that the binding of Adriamycin to RNA is reversible. Adriamycin was also found by gel electrophoresis to bind to yeast tRNA to form slow-migrating complexes. These results suggest that Adriamycin can inhibit RNA synthesis or processing by binding to RNA substrates.
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U2 - 10.1006/bbrc.1999.1815
DO - 10.1006/bbrc.1999.1815
M3 - Article
C2 - 10600508
AN - SCOPUS:0033590119
SN - 0006-291X
VL - 266
SP - 361
EP - 365
JO - Biochemical and biophysical research communications
JF - Biochemical and biophysical research communications
IS - 2
ER -