Silencing of RNA helicase II/Guα inhibits mammalian ribosomal RNA production

被引:69
作者
Henning, D
So, RB
Jin, RY
Lau, LF
Valdez, BC
机构
[1] Baylor Coll Med, Dept Pharmacol, Houston, TX 77030 USA
[2] Univ Illinois, Coll Med, Dept Mol Genet, Chicago, IL 60607 USA
关键词
D O I
10.1074/jbc.M310846200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The intricate production of ribosomal RNA is well defined in yeast, but its complexity in higher organisms is barely understood. We recently showed that down-regulation of nucleolar protein RNA helicase II/Gualpha (RH-II/Gualpha or DDX21) in Xenopus oocytes inhibited processing of 20 S rRNA to 18 S and contributed to degradation of 28 S rRNA (Yang, H., Zhou, J., Ochs, R. L., Henning, D., Jin, R., and Valdez, B. C. (2003) J. Biol. Chem. 278, 38847-38859). Since no nucleolar RNA helicase has been functionally characterized in mammalian cells, we used short interfering RNA to search for functions for RH-II/Gualpha and its paralogue RH-II/Gualpha in rRNA production. Silencing of RH-II/Gualpha by more than 80% in HeLa cells resulted in an almost 80% inhibition of 18 and 28 S rRNA production. This inhibition could be reversed by exogenous expression of wild type RH-II/Gualpha. A helicase-deficient mutant form having ATPase activity was able to rescue the production of 28 S but not 18 S rRNA. A phenotype exhibiting inhibition of 18 S and 28 S rRNA production was also observed when the paralogue RH-II/Gualpha was overexpressed. Both down-regulation of RH-II/Gualpha and overexpression of RH-II/Gualpha slowed cell proliferation. The opposite effects of the two paralogues suggest antagonistic functions.
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页码:52307 / 52314
页数:8
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共 51 条
[1]  
Andersen JS, 2002, CURR BIOL, V12, P1, DOI 10.1016/S0960-9822(01)00650-9
[2]   Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells [J].
Elbashir, SM ;
Harborth, J ;
Lendeckel, W ;
Yalcin, A ;
Weber, K ;
Tuschl, T .
NATURE, 2001, 411 (6836) :494-498
[3]  
FLORESROZAS H, 1993, J BIOL CHEM, V268, P21372
[4]   DBPA - A DEAD BOX PROTEIN SPECIFICALLY ACTIVATED BY 23S RIBOSOMAL-RNA [J].
FULLERPACE, FV ;
NICOL, SM ;
REID, AD ;
LANE, DP .
EMBO JOURNAL, 1993, 12 (09) :3619-3626
[5]   Nucleolin functions in the first step of ribosomal RNA processing [J].
Ginisty, H ;
Amalric, F ;
Bouvet, P .
EMBO JOURNAL, 1998, 17 (05) :1476-1486
[6]   Composition and functional characterization of yeast 66S ribosome assembly intermediates [J].
Harnpicharnchai, P ;
Jakovljevic, J ;
Horsey, E ;
Miles, T ;
Roman, J ;
Rout, M ;
Meagher, D ;
Imai, B ;
Guo, YR ;
Brame, CJ ;
Shabanowitz, J ;
Hunt, DF ;
Woolford, JL .
MOLECULAR CELL, 2001, 8 (03) :505-515
[7]   Proteomic analysis of human Nop56p-associated pre-ribosomal ribonucleoprotein complexes - Possible link between Nop56p and the nucleolar protein treacle responsible for Treacher Collins syndrome [J].
Hayano, T ;
Yanagida, M ;
Yamauchi, Y ;
Shinkawa, T ;
Isobe, T ;
Takahashi, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (36) :34309-34319
[8]   Active disruption of an RNA-protein interaction by a DExH/D RNA helicase [J].
Jankowsky, E ;
Gross, CH ;
Shuman, S ;
Pyle, AM .
SCIENCE, 2001, 291 (5501) :121-125
[9]   EXPRESSION, ISOLATION, AND CHARACTERIZATION OF THE HEPATITIS-C VIRUS ATPASE/RNA HELICASE [J].
JIN, L ;
PETERSON, DL .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1995, 323 (01) :47-53
[10]   Regulation of ribosome biogenesis within the nucleolus [J].
Leary, DJ ;
Huang, S .
FEBS LETTERS, 2001, 509 (02) :145-150