A new twist on RNA helicases: DExH/D box proteins as RNPases

Nature Structural Biology

Volumn 8, Issue 2, 2001, Pages 113-116

  Schwer, B ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; NUCLEOSIDE TRIPHOSPHATASE; RIBONUCLEOPROTEIN; RNA; RNA HELICASE;

HYDROLYSIS; PRIORITY JOURNAL; PROTEIN RNA BINDING; REVIEW; RIBOSOME; RNA SPLICING; RNA SYNTHESIS; RNA TRANSLATION;

ADENOSINE TRIPHOSPHATASES; AMINO ACID MOTIFS; ANIMALS; BASE SEQUENCE; RIBONUCLEOPROTEINS; RNA; RNA HELICASES; RNA SPLICING; RNA-BINDING PROTEINS; SPLICEOSOMES;

EID: 0035147544     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/84091     Document Type: Review

References (57)

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3. Helicase motifs: The engine that powers DNA unwinding
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5. Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase I, a DNA-dependent ATPase of the DExH box family
6. Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrotase II, a DExH box RNA helicase
7. The QRxGRxGR'G motif of the vaccinia virus DExH box RNA helicase NPH-II is required for ATP hydrolysis and RNA unwinding but not for RNA binding
8. A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein
9. The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication
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12. Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
13. Vaccinia virions lacking the RNA helicase nucleoside triphosphate phosphohydrolase II are defective in early transcription
14. The DExH protein NPH-II is a processive and directional motor for unwinding RNA
15. Vaccinia virus RNA helicase: Nucleic add specificity in duplex unwinding
16. Active disruption of an RNA-Protein interaction by a DExH/D RNA helicase
17. The DEAD box protein elF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
18. Mechanic devices of the spliceosome: Motors, clocks, springs, and things
19. The structure and function of proteins involved in mammalian pre-MRNA splicing
20. The question remains: Is the spliceosome a ribozyme?
21. Metal-Ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome
22. Dynamic RNA-RNA interactions in the spliceosome
23. RNA-RNA interactions in the spliceosome: Unraveling the ties that bind
24. The purified yeast pre-MRNA splicing factor PRP2 is an RNA-Dependent NTPase
25. Pre-MRNA splicing within an assembled yeast spliceosome requires an RNA-Dependent ATPase and ATP hydrolysis
26. PRP16 is an RNA-Dependent ATPase that interacts transiently with the spliceosome
27. A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis
28. Prp22, a DExH-Box RNA helicase, plays two distinct roles in yeast pre-MRNA splicing
29. The DEAH-Box protein PRP22 is an ATPase that mediates ATP-Dependent mRNA release from the spliceosome and unwinds RNA duplexes
30. Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD-Box splicing factor
31. Deletion of MUD2, the yeast homologue of U2AF65, can bypass the requirement for Sub2, an essential spliceosomal ATPase
32. Multiple roles for the yeast SUB2/yUAP56 gene in splicing
33. Identification and characterization of yUAP/Sub2p, a yeast homolog of the essential human pre-MRNA splicing factor hUAP56
34. Genetic interactions of conserved regions in the DEAD-Box protein Prp28p
35. In vitro reconstitution of mammalian U1 snRNPs active in splicing: The U1-C protein enhances the formation of early (E) spliceosomal complexes
36. Identification and characterization of a yeast homolog of U1 snRNP-Specific protein C
37. U1-Specific protein C needed for efficient complex formation of U1 snRNP with a 5′ splice site
38. An RNA switch at the 5′ splice site requires ATP and the DEAD box protein Prp28p
39. The human U5 snRNP-Specific 100-KD protein is an RS domain-Containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28p
40. The 100 kD U5 snRNP protein (hPrp28p) contacts the 5′ splice site through its ATPase site
41. PRP28, a 'DEAD-Box' protein, is required for the first step of pre-MRNA splicing in vitro
42. The MUD2 protein: An interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition
43. The splicing factor BBP interacts specifically with the pre-MRNA branchpoint sequence UACUAAC
44. A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition
45. Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-MRNA
46. The Saccharomyces cerevisiae Prp5 protein has RNA-Dependent ATPase activity with specificity for U2 small nuclear RNA
47. ATP can be dispensable for prespliceosome formation in yeast
48. U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-Branchpoint interaction
49. Vaccinia NPH-I, a DExH-Box ATPase, is the energy coupling factor for mRNA transcription termination
50. Vaccinia virus nucleoside triphosphate phosphohydrolase I is an essential viral early gene transcription termination factor
51. An engine for nucleosome remodeling
52. The yeast SNF2/SWI2 protein has DNA-Stimulated ATPase activity required for transcriptional activation
53. Functional analysis of the DNA-Stimulated ATPase domain of yeast SWI2/SNF2
54. The NMR structure of the 38 kDa U1A protein-PIE RNA complex reveals the basis for cooperativity in regulation of polyadenylation by human U1A protein
55. Prp43: An RNA helicase-Like factor involved in spliceosome disassembly
56. Identification of eight proteins that cross-Link to pre-MRNA in the yeast commitment complex