Protein displacement by DExH/D "RNA helicases" without duplex unwinding

被引:204
作者
Fairman, ME
Maroney, PA
Wang, W
Bowers, HA
Gollnick, P
Nilsen, TW [1 ]
Jankowsky, E
机构
[1] Case Western Reserve Univ, Dept Biochem, Cleveland, OH 44106 USA
[2] Case Western Reserve Univ, Sch Med, Ctr RNA Mol Biol, Cleveland, OH 44106 USA
[3] SUNY Buffalo, Dept Biol Sci, Buffalo, NY 14260 USA
关键词
D O I
10.1126/science.1095596
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Members of the DExH/D superfamily of nucleic acid-activated nucleotide triphosphatases are essential for virtually all aspects of RNA metabolism, including pre-messenger RNA splicing, RNA interference, translation, and nucleocytoplasmic trafficking. Physiological substrates for these enzymes are thought to be regions of double-stranded RNA, because several DExH/D proteins catalyze strand separation in vitro. These "RNA helicases" can also disrupt RNA-protein interactions, but it is unclear whether this activity is coupled to duplex unwinding. Here we demonstrate that two unrelated DExH/D proteins catalyze protein displacement independently of duplex unwinding. Therefore, the essential functions of DExH/D proteins are not confined to RNA duplexes but can be exerted on a wide range of ribonucleoprotein substrates.
引用
收藏
页码:730 / 734
页数:5
相关论文
共 26 条
[1]   Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA [J].
Antson, AA ;
Dodson, EJ ;
Dodson, G ;
Greaves, RB ;
Chen, XP ;
Gollnick, P .
NATURE, 1999, 401 (6750) :235-242
[2]   Posttranscription initiation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure [J].
Babitzke, P ;
Gollnick, P .
JOURNAL OF BACTERIOLOGY, 2001, 183 (20) :5795-5802
[3]   Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor [J].
Chen, JYF ;
Stands, L ;
Staley, JP ;
Jackups, RR ;
Latus, LJ ;
Chang, TH .
MOLECULAR CELL, 2001, 7 (01) :227-232
[4]   MOT1-catalyzed TBP-DNA disruption: uncoupling DNA conformational change and role of upstream DNA [J].
Darst, RP ;
Wang, DY ;
Auble, DT .
EMBO JOURNAL, 2001, 20 (08) :2028-2040
[5]   Direct measurement of single-stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine [J].
Dillingham, MS ;
Wigley, DB ;
Webb, MR .
BIOCHEMISTRY, 2002, 41 (02) :643-651
[6]   Messenger-RNA-binding proteins and the messages they carry [J].
Dreyfuss, G ;
Kim, VN ;
Kataoka, N .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2002, 3 (03) :195-205
[7]   Probing the relationship between RNA-stimulated ATPase and helicase activities of HCVNS3 using 2′-O-methyl RNA substrates [J].
Hesson, T ;
Mannarino, A ;
Cable, M .
BIOCHEMISTRY, 2000, 39 (10) :2619-2625
[8]   Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase [J].
Iost, I ;
Dreyfus, M ;
Linder, P .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (25) :17677-17683
[9]   The DExH protein NPH-II is a processive and directional motor for unwinding RNA [J].
Jankowsky, E ;
Gross, CH ;
Shuman, S ;
Pyle, AM .
NATURE, 2000, 403 (6768) :447-451
[10]   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