ライフサイエンスコーパス: RdRP

1 RdRPs are targets for antiviral drug development, but th

2 RdRPs have been proposed to act through a variety of mec

3 by an RNA-dependent RNA polymerase activity (RdRP).

4 tions in conserved motif A drastically alter RdRP fidelity, which can be either increased or decrease

5 We show that orthologs of QDE-1, an RdRP component of the quelling pathway in Neurospora cra

6 ng evidence that mammalian Pol II acts as an RdRP to control the stability of a cellular RNA by exten

7 e is the first example of a gene encoding an RdRP-related protein with an essential developmental fun

8 d shell protein (CSP) interacts with VP4 and RdRP.

9 Both RdRP recruitment and mRNA silencing require Argonaute pr

10 es from an independent de novo initiation by RdRP.

11 d by sequential use of downstream primers by RdRP.

12 ipts derived from cellular messenger RNAs by RdRP activity may have key roles in cellular regulation.

13 undant viral and host siRNAs by the cellular RdRPs.

14 nscriptional silencing using a single Dicer, RdRP, and Argonaute protein.

15 tes tightly with Dcr-2, similar to the Dicer-RdRP interaction observed in lower eukaryotes.

16 e for successive engagement of two different RdRPs in an endogenous siRNA-based mechanism targeting s

17 Here, we show that distinct RdRPs function sequentially to produce small RNAs that t

18 yze the function of a Caenorhabditis elegans RdRP, RRF-3, during spermatogenesis.

19 There are four C. elegans RdRPs, including two with known germline functions.

20 Among C. elegans RdRPs, we find that only EGO-1 is required for H3K9me2 e

21 cDNAs representing only two genes encoding RdRPs were identified in N. benthamiana.

22 Multiple active forms of the FCV RdRP were identified.

23 ng that Pro-Pol is an active form of the FCV RdRP.

24 e importance of the palm domain movement for RdRP active site closure and demonstrate that protein en

25 ining new interactions that are required for RdRP activity.

26 l highlighting the key features required for RdRP inhibition is proposed.

27 nteraction with L to form a fully functional RdRP.

28 fied and the cellular function of the Pol II RdRP activity is unknown.

29 lting from extension of B2 RNA by the Pol II RdRP can be removed from Pol II by a factor present in n

30 The individual RdRP subcomplex contains all the characterized motifs an

31 equence to the salicylic acid (SA)-inducible RdRP from Nicotiana tabacum required for defense against

32 iana plants transformed with an SA-inducible RdRP gene from Medicago truncatula were more resistant t

33 hese results strongly suggest that inducible RdRP activity plays an important role in plant antiviral

34 iana lacks an active SA- and virus-inducible RdRP and thus is hypersusceptible to viruses normally li

35 es differed from those of other SA-inducible RdRPs in that they contained a 72-nt insert with tandem

36 he biochemical characterization of influenza RdRP subcomplex comprising PA, PB1, and N terminus of PB

37 , as both a substrate and a template for its RdRP activity.

38 tein of RABV and the characterization of its RdRP activity in vitro The study provides a new assay th

39 system for study of this process, since its RdRP (VP1) is catalytically active and can specifically

40 tion of a capping enzyme with a picorna-like RdRP in the AfuTmV-1 genome is a striking case of chimer

41 D-elp1 is a noncanonical RdRP that can synthesize dsRNA from different ssRNA temp

42 Due to the general conservation of RdRP structures, these results suggest that the specific

43 We find that the bracelet domain of RdRP undergoes marked conformational change when q-CPV i

44 ine the requirements in P for stimulation of RdRP activity as residues 11 to 50 of P and formally dem

45 teraction between the PA and PB1 subunits of RdRP, we have designed and synthesized a series of analo

46 To further our understanding of RdRP function, we assembled, purified, and then crystall

47 g a new space in the chemical variability of RdRP inhibitors.

48 enger RNA (mRNA) leads to the recruitment of RdRPs and synthesis of secondary siRNAs using the target

49 to the active site had only minor effects on RdRP function, but the stacking interaction between Phe(

50 esis and the consequences of these events on RdRP function.

51 One RdRP was similar in sequence to SDE1/SGS2 required for m

52 We conclude that divergence of orthologous RdRPs can result in functional innovation while retainin

53 lls, copurifying proteins included the other RdRP subunits (PB1 and PA) and the viral nucleoprotein a

54 iral siRNAs by RNA-dependent RNA polymerase (RdRP) 1 (RDR1) and RDR6 and of the endogenous virus-acti

55 Plants contain RNA-dependent RNA polymerase (RdRP) activities that synthesize short cRNAs by using ce

56 ransferase and RNA-dependent RNA polymerase (RdRP) activities.

57 ported to have RNA-dependent RNA polymerase (RdRP) activity.

58 r complex, has RNA-dependent RNA polymerase (RdRP) activity.

59 g subunits: an RNA-dependent RNA polymerase (RdRP) and an NTPase VP4.

60 ies include an RNA-dependent RNA polymerase (RdRP) and an RNA endonuclease that cleaves capped primer

61 regenerated by RNA-dependent RNA polymerase (RdRP) and Dicer, but siRNAs from single-copy sequences a

62 ubstrate of PV RNA-dependent RNA polymerase (RdRP) and is incorporated into RNA mimicking both ATP an

63 d to the tomato RNA-directed RNA polymerase (RdRP) and to Neurospora crassa QDE-1, two proteins impli

64 that the viral RNA-dependent RNA polymerase (RdRP) complex can be an optimal target of protein-protei

65 e component of RNA-dependent RNA polymerase (RdRP) complexes essential for several distinct 22G-RNA s

66 ich encodes an RNA-dependent RNA polymerase (RdRP) containing a unique GDNQ motif normally characteri

67 her csr-1, the RNA-dependent RNA polymerase (RdRP) ego-1, or the dicer-related helicase drh-3, leads

68 R6, a putative RNA-dependent RNA polymerase (RdRP) from Arabidopsis thaliana, has previously been fou

69 lly within the RNA-dependent RNA polymerase (RdRP) gene.

70 The RNA-dependent RNA polymerase (RdRP) of nonsegmented negative-sense RNA viruses consist

71 assay for the RNA-dependent RNA polymerase (RdRP) of rabies virus (RABV).

72 e of the viral RNA-dependent RNA polymerase (RdRP) on host factors makes it a major host range determ

73 he error-prone RNA-dependent RNA polymerase (RdRP) or through genetic reassortment enables perpetuati

74 thesized by an RNA-dependent RNA polymerase (RdRP) requires the PIR-1 phosphatase.

75 by poliovirus RNA-dependent RNA polymerase (RdRP) revealed that 3-NPNTP was not accepted universally

76 ext, the viral RNA-dependent RNA polymerase (RdRP) subunits assembly has emerged as an attractive tar

77 y of a targeted RNA-directed RNA polymerase (RdRP) system that can convert a small population of exog

78 RRF-1, a worm RNA-dependent RNA polymerase (RdRP) that is known to produce single-stranded secondary

79 1 is a putative RNA-directed RNA polymerase (RdRP) that is required for multiple aspects of C. elegan

80 more than one RNA-dependent RNA polymerase (RdRP) that probably emerged as a result of gene duplicat

81 irally encoded RNA-dependent RNA polymerase (RdRP) that uses a unique palm domain active site closure

82 y requires the RNA-dependent RNA polymerase (RdRP) to use 10-12 different mRNAs as templates for (-)

83 depend on its RNA-dependent RNA polymerase (RdRP), composed of the PA, PB1, and PB2 subunits.

84 that SAD-1, an RNA-directed RNA polymerase (RdRP), is required for MSUD.

85 novo initiating RNA-directed RNA polymerase (RdRP), P2, forms the central machinery in the infection

86 t depletion of RNA-dependent RNA polymerase (RdRP)-derived secondary small RNAs termed 22G-RNAs.

87 and the RRF-3 RNA-dependent RNA polymerase (RdRP).

88 ute, dicer and RNA-dependent RNA polymerase (RdRP).

89 kinase and an RNA-dependent RNA polymerase (RdRP).

90 include viral RNA-dependent RNA polymerase (RdRP).

91 icivirus (FCV) RNA-dependent RNA polymerase (RdRP).

92 arget mRNAs by RNA-dependent RNA polymerase (RdRP).

93 virus-encoded RNA-dependent RNA polymerase (RdRP).

94 d by the viral RNA-dependent RNA polymerase (RdRP).

95 iated with the RNA-dependent RNA polymerase (RdRP).

96 sis requires an RNA-directed RNA polymerase (RdRP)].

97 Dicer (Dcr1), RNA-dependent RNA polymerase (RdRP; Rdp1), and Argonaute (Ago1).

98 certain viral RNA-dependent RNA polymerases (RdRP) synthesizing RNA on RNA templates.

99 by the viral RNA-dependent RNA polymerases (RdRP).

100 Endogenous RNA-directed RNA polymerases (RdRPs) are cellular components capable of synthesizing n

101 Cellular RNA-dependent RNA polymerases (RdRPs) function in development and RNA-mediated silencin

102 d the role of RNA-dependent RNA polymerases (RdRPs) in N. benthamiana antiviral defense.

103 The RNA-dependent RNA polymerases (RdRPs) of Cystoviridae bacteriophages, like those of euk

104 RNA-dependent RNA polymerases (RdRPs) of the Flaviviridae family catalyze replication o

105 ose essential RNA-dependent RNA polymerases (RdRPs) share a structurally homologous core with an enci

106 des, cellular RNA-dependent RNA polymerases (RdRPs) use AGO targets as templates for amplification of

107 es that act as RNA-directed RNA polymerases (RdRPs).

108 oth involving RNA-dependent RNA polymerases (RdRPs).

109 ng signals by RNA-dependent RNA polymerases (RdRPs).

110 tep involving RNA-dependent RNA polymerases (RdRPs).

111 We also find that RDE-8 promotes RdRP activity, thereby ensuring amplification of siRNAs.

112 t multiple loci spanning the viral protease, RdRP, and capsid ORFs and isolated individual recombinan

113 We purified RdRPs using a recombinant influenza virus in which the P

114 By comparing the properties of RABV RdRP with those of the related rhabdovirus, vesicular st

115 e replaced by those of VSV P stimulated RABV RdRP activity on naked RNA but was insufficient to permi

116 ts for template recognition by the rotavirus RdRP and compared those to the requirements for formatio

117 which targeting by ERGO-1 recruits a second RdRP (RRF-1 or EGO-1), which in turn transcribes 22G-RNA

118 nt antisense RNAs, dependent on a secondary RdRP (RRF-1) and associating with at least one distinct

119 Such RdRP paralogs often participate in distinct RNA silencin

120 We also found that RdRP recognition signals are distinct from cis-acting si

121 The structures indicate that RdRPs use a fully prepositioned templating base for nucl

122 The RdRP (protein P2) is assembled within the procapsid, and

123 The RdRP is contained within a viral large (L) protein, whic

124 The RdRP RRF-1 colocalizes with MUT-16 at Mutator foci, sugg

125 We show that DCR-1, the RdRP RRF-3, and the dsRNA-binding protein RDE-4 are requ

126 by limited structural information about the RdRP catalytic cycle.

127 Although the RdRP alone can specifically bind to viral mRNAs, our ana

128 vent efficient recognition of the RNA by the RdRP.

129 mRNA fragments to serve as templates for the RdRP-directed amplification of the silencing signal.

130 ting plant defense response also induced the RdRP activity, whereas biologically inactive analogs did

131 During infection, the RdRP replicates and transcribes the viral genome, which

132 at ribavirin triphosphate (RTP) inhibits the RdRP.

133 ely studied, the underlying mechanism of the RdRP complex is still unclear.

134 To determine the initial location of the RdRP inside the procapsid of bacteriophage Phi6, we perf

135 luenza virus in which the PB2 subunit of the RdRP is fused to a Strep-tag.

136 hance the initiation and processivity of the RdRP.

137 irectly or indirectly, with a subunit of the RdRP.

138 phorylated antisense RNAs that depend on the RdRP homolog RRF-3, the Argonaute ERGO-1, DICER, and a s

139 vely to form a unique functional site on the RdRP responsible for JAK-STAT inhibition.

140 ectron microscopy, we have reconstructed the RdRP tetramer complex at 4.3 A, highlighting the assembl

141 domain that is similar in appearance to the RdRP of dsRNA viruses and multiple accessory appendages

142 735 (of 903), a range which lies within the RdRP domain.

143 stretches of specific amino acids within the RdRP, 374 to 380 and 624 to 647, as critical for inhibit

144 rmally limited in their accumulation by this RdRP.

145 To elucidate the antiviral role of this RdRP in a different host plant and to evaluate whether p

146 icance of genetic diversity acquired through RdRP, we characterize an IAV fidelity variant derived fr

147 A tobacco RdRP gene, NtRDRP1, was isolated and found to be induced

148 ecently found that the activity of a tobacco RdRP was increased in virus-infected or SA-treated plant

149 The requirement for two RdRP/Argonaute combinations and initiation by a rare cla

150 To isolate the function of the viral RdRP (NS5) from that of other host or viral factors pres

151 ions induced by the recruitment of the viral RdRP and host factors to subcellular membrane microdomai

152 The viral RdRP is an important host range determinant, indicating

153 y with the PB1 and PB2 subunits of the viral RdRP, and small interfering RNA (siRNA)-mediated knockdo

154 oration of ribonucleotides into RNA by viral RdRPs, thus providing important considerations for the d

155 RNA virus replication by plant viral RdRPs occurs inside vesicle-like membrane invaginations

156 ins that interact with the influenza A virus RdRP in infected human cells.

157 egulates the activity of the influenza virus RdRP.

158 ch other when modeled on the West Nile virus RdRP crystal structure.

159 imental evidence shows that some plant virus RdRPs are able to perform replication in trans of genomi

160 ly conserved among positive-strand RNA virus RdRPs.

161 The in vitro RdRP assay system that utilizes cytoplasmic extracts fro

162 EN), a flavivirus family member, an in vitro RdRP assay was established using cytoplasmic extracts of

163 alen-UV cross-linking method and an in vitro RdRP assay, we analyzed structural determinants for phys

164 ssay is described here that utilizes the WNV RdRP and subgenomic (-)- and (+)-strand template RNAs co