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Enzyme Nomenclature
Information on EC 2.7.7.48 - RNA-directed RNA polymerase
for references in articles please use BRENDA:EC2.7.7.48
Word Map on EC 2.7.7.48
- 2.7.7.48
- viruses
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antiviral
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double-stranded
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rnaps
- bacteriophage
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single-stranded
- chromatin
- subtilis
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holoenzyme
- rrna
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virion
- infectious
- vaccine
- dsrnas
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helicase
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ribonucleoproteins
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interferon
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nascent
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dna-dependent
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polyproteins
- replicons
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footprint
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mosaic
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sequence-specific
- rifampicin
- nucleocapsids
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polyadenylation
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duplex
- dengue
- polya
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outbreak
- ribavirin
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non-nucleoside
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pre-mrnas
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supercoiled
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nucleolar
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virological
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stem-loops
- gastroenteritis
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non-structural
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nucleoprotein
- coronavirus
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anti-hcv
- dicer
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stall
-
unwind
- rotavirus
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virus-specific
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virus-like
- encephalitis
- medicine
- pharmacology
- drug development
- molecular biology
- analysis
- synthesis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.7.7.48
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RECOMMENDED NAME
GeneOntology No.
RNA-directed RNA polymerase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nucleoside triphosphate + RNAn = diphosphate + RNAn+1
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (RNA-directed)
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
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CAS REGISTRY NUMBER
COMMENTARY
9026-28-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. AaV-1, isolated from the mycelia of EGS 35-193 strain of Alternaria alternata
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i.e. BlVS, from Rubus canadensis berris, the virus might belong to the family Tymoviridae
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i.e. CsfrRNAV, from the cytosol of axenic clonal algal strain L-4 of the bloom-forming Chaetoceros socialis f. radians, isolated from surface water at the Itsukaichi fishing port in Hiroshima Bay, Japan
UniProt
i.e. ORMV, a tobamovirus taxonomically distinct from the type member of the genus, cultivated on Nicotiana benthamiana and Nicotiana tabacum plants
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i.e. FgV3, a dsRNA mycovirus from Fusarium graminearum strain DK3
UniProt
i.e. FgV4, a dsRNA mycovirus from Fusarium graminearum strain DK4
UniProt
i.e. GLRaV-Pr, an isolate from Greek grapevines, Vitis vinifera cv. Mantilaria, belongs to the Ampelovirus group
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i.e. IYSV, belongs to the genus Tospovirus, family Bunyaviridae, transmitted by onion thrips, Thrips tabaci
UniProt
Potato spindle tuber viroid (PSTVd) RNA genome in Solanum lycopersicum
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dsR1; i.e. PmV1, belongs to the genus Partitivirus, a plant-associated virus
UniProt
P2a-P2b fusion protein forming the viral RNA replicase; i.e. RuCMV, a sobemovirus, isolated from raspberry and bramble plants in north east Scotland
UniProt
i.e. TSV, isolated from tail muscle tissue of infected shrimp from shrimp farms in Texas in 2004, a member of the family Dicistroviridae
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i.e. TMV, is a type member of the tobamovirus family, clone TMV-KK1, cultivated on Nicotiana benthamiana and Nicotiana tabacum plants
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infected with Cowpea mosaic virus. The host-encoded enzyme is strongly stimulated upon CPMV infection of cowpea leaves
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643379, 643389, 643391, 643397, 643399, 643401, 643407, 661081, 662739, 672464, 672592, 673227, 675368, 690468, 690470, 690615, 692029, 721832, 723695, 737570, 738678
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genotype 1b isolate J4 with 21 amino acid C-terminal truncation and genotype 1b isolate RB01
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genotype-1b. HC-J4 NS5BDELTA21, a C-terminally truncated polymerase based on the consensus sequence of pCV-J4L6S
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standard activity strains A/WSN/33, H1N1, and A/NT/60/68, H3N2, and increased activity strains A/HongKong/156/97, H5N1, and A/Vietnam/1194/04, H5N1
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infected with alfalfa mosaic virus. The synthesis of the viral RNA is mediated by a pre-existing host enzyme, possibly modified by virus-coded proteins
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tobacco contains an RNA replicating capability, the amount of which is increased by infection with an RNA virus without noticeable changes in its enzymatic properties
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inoculated with potato spindle tuber viroid. In viroid-infected tomato leaf the activity of the host-encoded RdRP is significantly increased. Viroids are not translated into proteins so that they cannot code for a viroid-specific RNA replicase
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i.e. SINV-3, Argentinean isolate from the Santa Fe region of Argentina
UniProt
i.e. SINV-3, from a colony in the United States, DM isolate
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the RDR gene family, phylogenetic analysis of RDR genes present in potato and in a range of other plant species, overview
malfunction
metabolism
physiological function
additional information
malfunction
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RRF-3 mutation is involved in compromised spermatogenesis, that accounts for reduced brood size and X-chromosome loss from rrf-3 mutant hermaphrodites
malfunction
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mutations in the hepatitis C virus polymerase that increase RNA binding can confer resistance to cyclosporine A, an inhibitor that is used as therpeutic against HCV-induced acute and chronic liver disease
malfunction
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impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm
malfunction
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D-elp1 depletion inhibits RNAi in S2 cells but does not affect micro RNA function. In D-elp1 null third instar larvae transposon RNA levels are also increased and the corresponding transposon antisense RNAs are reduced
malfunction
in deletion strains of the RNA-dependent RNA polymerase RrpC, full-length and shorter retrotransposable element DIRS-1 (Dictyostelium intermediate repeat sequence 1) messenger RNAs are strongly enriched, shorter versions of long non-coding RNA in DIRS-1 antisense orientation are also enriched in rrpC- strains. DIRS-1 misregulation in the absence of RrpC leads to retrotransposon mobilization
malfunction
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suppression of Nicotiana benthamiana canonical 9-zinc finger transcription factor TFIIIA-7ZF reduces PSTVd replication, and overexpression of TFIIIA-7ZF enhances PSTVd replication in planta
malfunction
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silencing SlRDR1 using virus-induced gene silencing system significantly reduces SlRDR1 expression and tomato defense against tobacco mosaic virus but has no evident effect on alternative oxidase SlAOX1a transcription
malfunction
StRDR1 transcript accumulation decreases in transgenic potato plants constitutively expressing a hairpin construct. These plants when challenged with three viruses, potato virus Y, potato virus X, and tobacco mosaic virus show no increase in the susceptibility of potato to these viruses. Suppression of StRDR1 gene expression does not increase in the susceptibility to the viruses
malfunction
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RRF-3 mutation is involved in compromised spermatogenesis, that accounts for reduced brood size and X-chromosome loss from rrf-3 mutant hermaphrodites
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malfunction
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in deletion strains of the RNA-dependent RNA polymerase RrpC, full-length and shorter retrotransposable element DIRS-1 (Dictyostelium intermediate repeat sequence 1) messenger RNAs are strongly enriched, shorter versions of long non-coding RNA in DIRS-1 antisense orientation are also enriched in rrpC- strains. DIRS-1 misregulation in the absence of RrpC leads to retrotransposon mobilization
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metabolism
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Pol IV functions independently of the small RNA accumulation facilitated by RMR1 and RDR2. RMR1, RNA-directed DNA methylation factor, acts upstream of the RNA-dependent RNA polymerase, RDR2. While transposon-like sequences may be a common target of the maize RdDM pathway, the RMR1 and RDR2 proteins act differently with respect to their roles in mediating the type of trans-regulation induced by inverted repeats
metabolism
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the salicylic acid-induced viral defense in plants is distinct from the pathways mediating bacterial and fungal defense, which is pathogenesis-related protein-independent but involves an RNA-dependent RNA polymerase 1 (RDR1)-mediated RNA silencing mechanism and/or an alternative oxidase (AOX)-associated defense pathway. As the RDR1-mediated RNA silencing pathway and the AOX-regulated pathway are both involved in the salicylic acid-induced defense against viruses but are independent of pathogenesis-related protein genes, crosstalk between these two antiviral pathways may exist
physiological function
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RdRps are unique in that they create dsRNA by initiating polymerization at the 3' end of the substrate
physiological function
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RRF-3 is required for spermatocyte cell division, overview
physiological function
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the FHV RNA-dependent RNA polymerase, protein A, is the only viral protein necessary for genome replication in the budding yeast Saccharomyces cerevisiae
physiological function
the enzyme is responsible for replication and transcription of the eight separate segments of the viral RNA genome in the nuclei of infected cells
physiological function
Q9LKP0
RDR6 functions in trans-acting short interfering RNA, ta-siRNA, production. Positive regulators or effectors of SI and pistil development are regulated by ta-siRNAs, regulation, overview
physiological function
RDRs play a key role in RNA silencing, heterochromatin formation and natural gene regulation. It may play an important role in response to biotic and abiotic stresses
physiological function
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the enzyme is required for the RNA-directed DNA methylation, dedicated to the methylation of target sequences, which include transposable elements, regulatory regions of several protein-coding genes, and 5S rRNA-encoding DNA arrays. Pol IV, RDR2, DRM2, and Pol V, actors of the RdDM, are required to maintain a transcriptional silencing of 5S RNA genes at chromosomes 4 and 5, regulation, overview
physiological function
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small RNA deep sequencing reveals a functional role for RDR in promoting viral siRNA biogenesis through distinct mechanisms, overview. RDR1and RDR6 are also implicated in antiviral defense
physiological function
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D-elp1 is required for RNA interference, interacts with Dcr-2 protein, and has a role in transposon suppression, overview. It might be interacting with components of the RISC
physiological function
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the enzyme is required for replication of the genomes of positive-strand RNA viruses occuring in highly oligomeric complexes on the cytosolic surfaces of the intracellular membranes of infected host cells
physiological function
expression in Drosophila melanogaster enhances transitive dsRNA-dependent silencing; expression in Drosophila melanogaster triggers transcriptional silencing of unpaired DNA during embryonic mitosis. Isoform ego-1 triggers dsRNA-independent silencing, specifically of transgenes. The strain w, da-Gal4, UAST-ego-1, constitutively expressing ego-1, is capable of silencing transgene including dsRNA hairpin upon a single cross
physiological function
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isoform RDR6 is required for efficient hpRNA-induced RNA silencing in plants. Generation of wild-type and rdr6-11 Arabidopsis thaliana lines expressing green fluorescent protein and transformation with a green fluorescent protein-RNA interference construct leads to almost complete silencing of green fluorescent protein expression in the T1 generation of most green fluorescent protein-RNAi-transformed wild-type lines, whereas various levels of green fluorescent protein expression remain among the green fluorescent protein-RNAi-transformed rdr6-11 lines. Homozygous expression of green fluorescent protein-RNAi in the T3 generation is not sufficient to induce complete green fluorescent protein silencing in several rdr6-11 lines
physiological function
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Nicotiana benthamiana transformed with isoform RDR1 from Nicotiana tabacum exhibits hypersusceptibility to plum pox potyvirus and other viruses, resembling RDR6-silenced Nicotiana benthamiana. Nicotiana tabacum-RDR1 possesses silencing suppression activity and does not interfere with isoform RDR6-dependent siRNA accumulation but turns out to suppress RDR6-dependent sense-transgenes Isoform RDR1 might have a dual role, contributing, on one hand, to salicylic acid-mediated antiviral defense, and suppressing, on the other hand, the RDR6-mediated antiviral RNA silencing
physiological function
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systematic analysis of susceptibility and small RNA formation in Arabidopsis mutants lacking combinations of RNA-dependent RNA polymerase isoforms and dicer-like proteins. The vast majority of turnip mosaic virus-derived small interfering RNAs are dependent on dicer-like protein isoform DCL4 and RNA polymerase isoform RDR1, although full antiviral defense also requires isoforms DCL2 and RDR6. DCL4 is sufficient for antiviral silencing in inoculated leaves, but isoforms DCL2 and DCL4 are both involved in silencing in systemic tissues. Basal levels of antiviral RNA silencing and siRNA biogenesis are detected in mutants lacking isoforms RDR1, RDR2, and RDR6, indicating an alternate route to form double-stranded RNA that does not depend on the three previously characterized RNA-dependent RNA polymerase proteins; systematic analysis of susceptibility and small RNA formation in Arabidopsis mutants lacking combinations of RNA-dependent RNA polymerase isoforms and dicer-like proteins. The vast majority of turnip mosaic virus-derived small interfering RNAs are dependent on dicer-like protein isoform DCL4 and RNA polymerase isoform RDR1, although full antiviral defense also requires isoforms DCL2 and RDR6. DCL4 is sufficient for antiviral silencing in inoculated leaves, but isoforms DCL2 and DCL4 are both involved in silencing in systemic tissues. Basal levels of antiviral RNA silencing and siRNA biogenesis are detected in mutants lacking isoforms RDR1, RDR2, and RDR6, indicating an alternate route to form double-stranded RNA that does not depend on the three previously characterized RNA-dependent RNA polymerase proteins
physiological function
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isoform RDR6 acts in the biogenesis of various types and sizes of small RNAs. An rdr6-1 mutant, which is temperature sensitive and shows spikelet defects, displays reduced accumulation of trans-acting siR-auxin response factors, the conserved trans-acting siRNAs derived from the TAS3 locus, and ectopic expression of trans-acting siR-auxin response factors target genes. 21-Nucleotide phased small RNAs are also largely dependent on isoform RDR6. Isoform RDR6 has a strong impact on the accumulation of 24-nt phased small RNAs, but not on unphased ones
physiological function
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RNA polymerase II acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Mammalian Pol II acts as an RdRP to control the stability of a cellular RNA by extending its 3'-end. Extended B2 RNA can repress transcription, but with decreased potency
physiological function
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probing of the entire Dengue genome for interactions via Y3H with viral RNA-dependent RNA polymerase reveals a dominant interaction as a loop-forming ACAG motif in the 3' positive-stranded terminus, RdRp recognizes the top loop of 3'-SL in both genomic forms, interactions sites coincides with known flaviviral recombination sites inside the viral protein-coding region. Specific recognition of the RNA element occurs via an arginine patch in the C-terminal thumb domain of enzyme RdRp. Disruption of the interaction results in loss of viral replication ability in cells. This unique RdRp-RNA interface is found throughout flaviviruses
physiological function
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segment 2 (S2)-encoded RNA-dependent RNA polymerase (RdRp) helps the virus to propagate its genome in the host cell of the silkworm, Antheraea mylitta
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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negative-sense RNA viruses, such as influenza, encode large, multidomain RNA-dependent RNA polymerases that can both transcribe and replicate the viral RNA genome. Replication occurs through de novo initiation and involves a complementary RNA intermediate
physiological function
the RNA-dependent RNA polymerase RrpC silences the centromeric retrotransposon DIRS-1 post-transcriptionally and is required for the spreading of RNA silencing signals. RrpC is a key player in the silencing of centromeric retrotransposon DIRS-1. RrpC acts at the post-transcriptional level and is involved in spreading of RNA silencing signals, both in the 5' and 3' directions
physiological function
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the DNA-dependent RNA polymerase (DdRP) from Potato spindle tuber viroid (PSTVd) RNA genome in Solanum lycopersicum possesses RNA-dependent RNA polymerase activity. A land plant-specific transcription factor directly enhances transcription of a pathogenic noncoding RNA template by DNA-dependent RNA polymerase II
physiological function
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enzyme RDR1 is involved in the AOXmediated defense pathway against tobacco mosaic virus infection and plays a crucial role in enhancing RNA silencing to limit virus systemic spread
physiological function
mechanism of viruses attacking hosts whereby picornaviral 3D polymerase (3Dpol) enters the nucleus and targets the central pre-mRNA processing factor 8 (Prp8) to block premRNA splicing and mRNA synthesis. The 3Dpol inhibits the second catalytic step of the splicing process, resulting in the accumulation of the lariat-form and the reduction of the mRNA. 3Dpol inhibits intracellular pre-mRNA splicing by interacting with Prp8, modelling, overview
physiological function
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viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription
physiological function
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viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription
physiological function
the RNA-dependent RNA polymerase activity resides in the C-terminal two-thirds of non-structural protein (NS) 5 responsible for the de novo synthesis of the viral RNA genome. RdRp specifically binds to the viral UTR
physiological function
P2, an RNA-directed polymerase (RdRp), is the critical component of a four-protein polymerase complex (PX) that includes in addition to P2, the major capsid protein, P1, a packaging NTPase, P4, and an accessory protein, P71. P2 performs the dual tasks of transcription and replication de novo without the use of a primer (i. e. P2 is a self-priming RdRp), and plays a critical role in the cystoviral life cycle
physiological function
cellular RNA-dependent RNA polymerases catalyze synthesis of double-stranded RNAs that can serve to initiate or amplify RNA silencing. Enzyme RDR1 contributes to basal virus resistance in several plants
physiological function
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the RNA-dependent RNA polymerase of rice stripe virus is critical for both the transcription and replication of the viral genome
physiological function
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RRF-3 is required for spermatocyte cell division, overview
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physiological function
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the RNA-dependent RNA polymerase RrpC silences the centromeric retrotransposon DIRS-1 post-transcriptionally and is required for the spreading of RNA silencing signals. RrpC is a key player in the silencing of centromeric retrotransposon DIRS-1. RrpC acts at the post-transcriptional level and is involved in spreading of RNA silencing signals, both in the 5' and 3' directions
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physiological function
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mechanism of viruses attacking hosts whereby picornaviral 3D polymerase (3Dpol) enters the nucleus and targets the central pre-mRNA processing factor 8 (Prp8) to block premRNA splicing and mRNA synthesis. The 3Dpol inhibits the second catalytic step of the splicing process, resulting in the accumulation of the lariat-form and the reduction of the mRNA. 3Dpol inhibits intracellular pre-mRNA splicing by interacting with Prp8, modelling, overview
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physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
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physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
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physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
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physiological function
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the enzyme is responsible for replication and transcription of the eight separate segments of the viral RNA genome in the nuclei of infected cells
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additional information
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efficient polymerase assembly is a limiting factor in the viability of reassortant viruses, mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview
additional information
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the RNA polymerase of influenza virus is a heterotrimeric complex of PB1, PB2 and PA subunits, which cooperate in the transcription and replication of the viral genome
additional information
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viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements, birnaviral RdRP contains a K+-binding site within its palm subdomain. In most known polymerases, the conservative elements are arranged in alphabetical order, but variants with non-canonical sequence in the primarystructure also exist. In this way the polymerases of birnaviruses and some insect viruses possess elements of the active site in the order: C-A-B-D-E-F. Motif F carries conservative basic lysine and arginine residues that may be involved in the binding of RNA polymerase of birnaviruses. In birnavirus polymerases a serine residue located in the fingers subdomain can be subjected to guanidylation that birnavirus RdRP requires for self-priming. The thumb subdomain of birnaviral RdRP is close in size to the latter and also consists of four alpha-helices and small beta-sheet, which interacts with two beta-strands of the palm subdomain. The C-terminal subdomains of birnaviral polymerase represents an extra, expanded region with several alpha-helices not assembled into compact structure, and interact with the thumb subdomain and fingertips
additional information
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viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. The Gly64 in the polymerase molecule binds through hydrogen with N-terminal Gly1, which, in turn, interacts with the amino acid residues from the fingers subdomain (Ala239 and Leu241). Formation of the active site by palm conservative elements
additional information
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viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements
additional information
-
viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements. Molecular dynamics of hepatitis C virus RdRP, when interacting with the molecule of a specific inhibitor that binds to the thumb subdomain, show that the ligand binding significantly reduces the ability of the polymerase to change its conformation
additional information
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treatment of cells with a-amanitin or actinomycin D revealed that extension of B2 RNA by Pol II destabilizes the RNA
additional information
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phase-distributed sRNAs are identified within the dsRNA-seq read-covered regions. sRNA sequences from Col-0 (GSM121455, GSM154336, and GSM154375) are mapped onto the sequence regions with two or more phase-distributed, RDRdependent sRNA loci
additional information
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overall enzyme structure analysis from crystal structure, PDB IDs 3N6L, 3N6N, and 3N6M, conformational changes in the B-loop of RdRP. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
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overall enzyme structure analysis from crystal structure, PDB ID 1WNE. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
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overall enzyme structure analysis from crystal structure, PDB IDs 2XXD and 4E76. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
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overall enzyme structure analysis from crystal structure, PDB IDs 2PUS and 2R70. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
additional information
overall enzyme structure analysis from crystal structure, PDB ID 3ZED. Structure solution of RdRP-RNA-rNTP complexes, open and closed conformations of the B-loop in IBDV VP, overview
additional information
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overall enzyme structure analysis from crystal structures, PDB IDs 1SH0, 3BSO, and 1SH3. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
additional information
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polymerase FluPol is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding and endonuclease domains required for transcription initiation by cap-snatching. Comparison of apo-FluPolC with promoter-bound FluPolA, overview
additional information
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seven RdRP elongation complex structures derived from a crystal lattice that allows three RdRP nucleotide addition cycle (NAC) events. NTP recognition and translocation mechanisms in viral RdRPs and uniqueness of the viral RdRPs compared with other processive polymerases, modelling, overview. Determination of initial NTP binding, active site closure, and, in particular the RNA motion during translocation that shows an asymmetric movement of the two strands in the template-product duplex
additional information
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several structural states of the poliovirus RdRP nucleotide addition cycle (NAC) reveal a unique palm domain-based active site closure mechanism and propose a six-state NAC model including a hypothetical state representing translocation intermediates. NTP recognition and translocation mechanisms in viral RdRPs and uniqueness of the viral RdRPs compared with other processive polymerases, modelling, overview
additional information
structure of P2, the self-priming RdRp from cystovirus phi12, crystal structure analysis, overview. The tunnel through which template ssRNA accesses the active site is partially occluded by a flexible loop; this feature, along with sub-optimal positioning of other structural elements that prevent the formation of a stable initiation complex, indicate an inactive conformation in crystallo
additional information
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the RNA-dependent RNA polymerase (RdRp) in equine arteritis virus is expressed as the C-terminal domain of nonstructural protein 9 (nsp9)
additional information
the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
additional information
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phase-distributed sRNAs are identified within the dsRNA-seq read-covered regions. sRNA sequences from Col-0 (GSM121455, GSM154336, and GSM154375) are mapped onto the sequence regions with two or more phase-distributed, RDRdependent sRNA loci
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additional information
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overall enzyme structure analysis from crystal structure, PDB ID 1WNE. Structure solution of RdRP-RNA-rNTP complexes, overview
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additional information
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overall enzyme structure analysis from crystal structure, PDB IDs 2XXD and 4E76. Structure solution of RdRP-RNA-rNTP complexes, overview
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additional information
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overall enzyme structure analysis from crystal structure, PDB IDs 2PUS and 2R70. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
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additional information
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the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(dT)12 + UTP
diphosphate + ?
-
assay uses poly(A) as an RNA template and oligo(dT)12-18 as the primer. Enzyme is strictly dependent on the presence of primer
-
-
?
5-fluorouridine triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme incorporates 5-fluorouridine monophosphate during RNA elongation in place of UMP or CMP using homopolymeric and heteropolymeric templates. Incorporation of 5-fluorouridine monophosphate does not prevent chain elongation, and, in some sequence contexts, it favors misincorporations at downstream positions. 5-Fluorouridine monophosphate is incorporated into the nascent RNA and occupies the new 3'-end of the primer at the active site of the enzyme. 5-Fluorouridine monophosphate establishes a Watson and Crick pair with the corresponding acceptor AMP in the template strand and an additional hydrogen bond with Ser304 of the polymerase. Further interactions, similar to those observed with standard nucleotides, contribute also to stabilize 5-fluorouridine monophosphate in the 3'-terminus of the RNA. When present in the template, 5-fluorouridine monophosphate directs the incorporation of AMP and GMP, with ATP being a more effective substrate than GTP. The misincorporation of GMP is 17fold faster opposite 5-fluorouridine than opposite U in the template. But Incorporated 5-fluorouridine monophosphate is not a chain terminator during RNA elongation
RNA with incoporated 5-fluorouridine phosphate
-
?
ribavirin triphosphate + RNAn
?
ribavirin is a guanosine analogue that can be a substrate for the viral RNA polymerase. HCV is genetically variable, and this genetic variation can affect the polymerase's use of ribavirin triphosphate, overview
-
-
?
GTP + poly(C)
diphosphate + ?
-
use of poly(C) as template annealed with oligoG12 as primer
-
-
?
GTP + poly(C)
diphosphate + ?
-
use of poly(C) as template annealed with oligoG12 as primer
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
in addition to RNA-dependent RNA polymerase activity the enzyme also possesses cap-snatching capacity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme should be involved in the replication of BaMV
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
full-length negative strand BBV RNAs are synthesized
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme synthesizes single-stranded RNA transcripts of one polarity which are identical in size to the denatured parental double-stranded RNA segments
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is active in an in vitro RNA polymerase assay using homopolymeric RNA or BVDV minigenomic RNA templates. The major product is a covalently linked double-stranded molecule. In addition, a nucleotide-nonspecific and template-independent terminal nucleotidyl transferase activity is observed
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
dependent on and specific for BMV RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAs of Brome mosaic virus and the closely related cowpea Chlorotic mottle virus are the most effective, but some activity is also shown by certain other viral nucleic acids and polyribonucleotides
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
using poly(rA)/(dT)15 as a template-primer system
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
using poly(rA)/(dT)15 as a template-primer system
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is completely dependent on exogenous template. The enzyme utilizes a variety of viral RNAs and CMV satellite RNA as template for minus-strand synthesis. Cellular RNAs are not used as templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme copies CMV RNA and several other viral RNAs, Brome mosaic virus RNA, Alfalfa mosaic virus RNA and Tobacco mosaic virus RNA. Activity with poly(C) and poly(U) but not poly(A) or poly(G). The product with CMV RNA as template is heterogenous in size with a peak length of about 150 residues
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP + CMV RNA, yeast RNA or poly(C)
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q6DLV0
homopolymer C as the template and biotinoligo(G)20 as the primer
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q6DLV0
using homopolymer C as the template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
enzyme initiates RNA synthesis in a primer- and poly(A)-dependent manner in vitro
product is double-stranded RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme does not manifest strict specificity towards EMC RNA template. It can use also Qbeta RNA, rRNA of BHK cells or poly(C)
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
poly(A)-dependent oligo(U)-primed poly(U) polymerase activity. In the presence of an oligo(U) primer, the enzyme catalyzes the synthesis of a full-length copy of either poliovirus or globin RNA templates. In the absence of added primer, RNA products up to twice the length of the template are synthesized
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
kinetic mechanism for single nucleotide incorporation catalyzed by poliovirus polymerase in presence of Mg2+
-
-
r
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RdRP incorporation of incorrect nucleosides is inefficient, making precise determination of kinetic parameters experimentally challenging. The fidelity for poliovirus polymerase 3Dpol ranges from 12000 to 1000000 for transition mutations and 32000 to 43000000 for transversion mutations
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
VPg (a peptide comprising the 3B region of protein 3AB) is the 22-residue soluble product of 3AB cleavage and serves as the protein primer for RNA replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
substrate is HP1 RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
when the nucleotide concentrations are low, C is incorporated at the fastest rate and G at the slowest. G-incorporation step largely limits the overall reaction rate
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
composed of one phage-coded polypeptide and three host-supplied polypeptides which function in the biosynthesis of proteins in the uninfected host. Two of theses polypeptides, protein elongation factors EF-Tu and EF-Ts, are required for initiation of transcription by replicase with all templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
Qbeta replicase is an RNA-dependent RNA polymerase responsible for replicating the RNA genome of coliphage Qbeta and plays a key role in the life cycle of the Qbeta phage
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
kinetic model for the RNA replication reaction
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
purified recombinant FMDV 3D is active in polymerization assays using homopolymeric and heteropolymeric primer templates and in binding to RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
inducible enzyme
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
ATP, the enzyme requires a single-stranded molecule of RNA or polyribonucleotide as template, initiates new chains with purine ribonucleoside triphosphates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
661081, 662733, 672616, 673227, 690468, 690470, 690478, 690615, 691255, 691257, 691273, 692029, 693537, 695258
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
polyC/oligoG is more efficient in supporting the HCV NS5B polymerase activity than polyA/oligodT. PolyA/oligoU or polyI/oligodC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme performs RNA- or DNA oligonucleotide primer-dependent RNA synthesis on templates with a blocked 3' end or on homopolymeric templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
ribonucleotide-incorporating activity on an in vitro transcribed RNA containing the 3' end of the HCV genome. It also possesses ribunucleotide incorporation activity, to a lesser extent, on in vitro transcribed foreign RNA templates when RNA or DNA primers are present. The activity is higher with DNA primers than with RNA primers
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNA-dependent RNA polymerase activity uses poly(C) most efficiently as a template but is inactive on poly(U) and poly(G). The enzyme is able to copy a full-length or nearly full-length genome in the absence of additional viral or cellular cofactors. Poly(C)-oligo(G)12 is the most efficient substrate
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
once synthesis has begun, the C-terminally truncated enzyme NS5B(DELTA21) does not dissociate from the template until a complete double strand copy of the RNA is made
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
replication of Hepatitits C virus is thought to proceed via the initial synthesis of a complementary (-)RNA strand, which serves, in turn, as a template for the production of progeny (+)-strand RNA molecules. An RNA-dependent RNA polymerase is postulated to be involved in these steps
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
essential catalytic enzyme for HCV replication. NS5A binds RNA-dependent RNA polymerase and modulates RNA-dependent RNA polymerase activity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
NS5B RdRp is essential for viral replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
poly(C) RNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
nculeotides are GTP, CTP, ATP, and UTP, the RNA templates for the enzyme assay are transcribed from linearized murine inducible nitric oxide synthase, iNOS, clone having 400 nt insert in an in vitro transcription reaction using SP6 RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
B2 RNA is a substrate for RNA dependent RNA polymerization by Pol II
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
B2 RNA is a substrate for RNA dependent RNA polymerization by Pol II. Extension of B2 RNA by Pol II occurs from the 3'-end and is internally templated and requires all four NTPs, mechanism, overview. No activity with B2 RNA mutated at C155 to G
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in presence of Mg2+ significant activity is observed when poly(A) or poly(C) is used as template and the activity is template and primer-dependent. Poly(G) and poly(U) templates are not efficient substrates. Biotinylated oligoDNA primers appear to work slightly more efficiently than oligoRNA primers. In presence of Mn2+ activity is stimulated 2.5-5.6fold. RNA synthesis using poly(C) as template becomes primer-independent
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNA polymerase activity on homopolymeric templates poly(A) and poly(C) and heteropolymeric RNA templates primed with either RNA or DNA oligonucleotide primers or self-primed by a copy-back mechanism
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
required for replication of the HRV RNA genome
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in vitro transcription using the model RNA template, v84
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
various RNA substrates: Alu RNA, 110 nucleotides of the Alu domain of Pyrococcus horikoshii SRP RNA, Candida albicans tRNAAsn, U-rich RNA (59-GGCCAUCCUGU7 CCCU11CU19-39)29, ph-RNA of 81 nucleotides30, and short ph-RNA of 36 nucleotides comprising just the conserved 3' and 5' ends with a short linker and circular single stranded DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
various RNA substrates: Alu RNA, 110 nucleotides of the Alu domain of Pyrococcus horikoshii SRP RNA, Candida albicans tRNAAsn, U-rich RNA (59-GGCCAUCCUGU7 CCCU11CU19-39)29, ph-RNA of 81 nucleotides30, and short ph-RNA of 36 nucleotides comprising just the conserved 3' and 5' ends with a short linker and circular single stranded DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
replication occurs through de novo initiation and involves a complementary RNA intermediate
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates, indicating that the JEV NS5 protein is involved in regulating the ratio of positive strand RNA to negative strand RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the NS5 protein is able to use both plus- and minus-strand 3'-untranslated regions of the JEV genome as templates in the absence of a primer, with the latter RNA being a better template. Analysis of the RNA synthesis initiation site using the 3'-end 83 nucleotides of the JEV genome as a minimal RNA template reveals that the NS5 protein specifically initiates RNA synthesis from an internal site, U81, at the two nucleotides upstream of the 3'-end of the template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
poly(A) RNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
uses JEV and dengue-2 virus 3' end plus- and minus-strand RNA templates, the incorporation of [32P]-UMP is much lower when using positive-strand RNA as template than when using negative-strand RNA - an almost 10fold difference in efficiency
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
primer-free initiation assay with 13-nt RNA template, and ATP, CTP, FAM-UTP, and GTP, and additionally with a primer (5'-GUUCACACAGAUAAACUUCU-3') with a 6-FAM-labeled at the 5'-end in the primer extension assay
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates, indicating that the JEV NS5 protein is involved in regulating the ratio of positive strand RNA to negative strand RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
uses JEV and dengue-2 virus 3' end plus- and minus-strand RNA templates, the incorporation of [32P]-UMP is much lower when using positive-strand RNA as template than when using negative-strand RNA - an almost 10fold difference in efficiency
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
primer-free initiation assay with 13-nt RNA template, and ATP, CTP, FAM-UTP, and GTP, and additionally with a primer (5'-GUUCACACAGAUAAACUUCU-3') with a 6-FAM-labeled at the 5'-end in the primer extension assay
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
incorporation is more dependent on exogenopus UTP and GTP than ATP or CTP
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
incorporation is more dependent on exogenopus UTP and GTP than ATP or CTP
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
La France isometric virus
-
the enzyme is probably a transcriptase engaged in the synthesis of ssRNA transcripts corresponding to each of the virion-associated dsRNAs
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the polymerase product anneals only to measles RNA and not to Vero cell RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme catalyzes cap methylation of virus-specific mRNA as well as RNA synthesis
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
viral ribonucleoprotein complexes and purified recombinant L protein but not P protein exhibit mRNA (guanine-7-)methyl-transferase activity. mRNA synthesis in a reconstituted transcription system using purified N protein-genomic RNA complex as a template requires both the L and P proteins. Enzymatic properties of Senda virus mRNA (guanine-7-)methyl-transferase are different to that of cellular mRNA (guanine-7-)methyl-transferase. Unlike cellular enzyme, the SeV enzyme preferentially methylates capped RNA containing the viral mRNA 5'-end sequences (GpppApGpG-). The C-terminal part (amino acid residues 1,756–2,228) of the L protein catalyzes cap methylation, whereas the N-terminal half (residues 1–1,120) containing putative RNA polymerase subdomains does not
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the random polymers poly(UG), poly(UC), poly(AG) and poly(AU) serve as more effective templates than homopolymers
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
NV 3Dpol yields two different products when incubated with synthetic RNA in vitro: (1) a double-stranded RNA consisting of two single strands of opposite polarity or (2) the single-stranded RNA template labelled at its 39 terminus by terminal transferase activity. Initiation of RNA synthesis by NV 3Dpol on heteromeric RNA template occurs de novo
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the polymerase structure is switchable, with a discrete set of contacts stabilizing the initiation-competent form of the enzyme so that relatively modest changes can have-range effects, controlling the switch from the initiation to elongation phase, with premature conformational switching producing a structure that preferentially initiates by back-priming
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is RNA, the phi6 polymerase is highly processive and can use either single- or double-stranded RNA as a template and synthesizes a full-length complementary strand of an RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
NTPs are ATP, GTP, CTP, and UTP, roles of the negatively charged plough area on the polymerase surface, of the rim of the template tunnel and of the template specificity pocket that is key in the formation of the productive RNA-polymerase binary complex. The positively charged rim of the template tunnel has a significant role in the engagement of highly structured ssRNA molecules, whereas specific interactions further down in the template tunnel promote ssRNA entry to the catalytic site
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
key enzyme of replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in a synthetic RNA template-dependent reaction, sapovirus 3Dpol synthesizes a double-stranded RNA or labels the template 3' terminus by terminal transferase activity. Initiation of RNA synthesis occurs de novo on heteropolymeric templates or in a primer dependent manner on polyadenylated templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme synthesizes single-stranded RNA transcripts of one polarity which are identical in size to the denatured parental double-stranded RNA segments
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
nsP4 possesses the RNA-dependent RNA polymerase activity required for the replication of the SIN genome and transcription of a subgenomic mRNA during infection
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in the absence of other viral proteins nsP4 is capable of copying SIN plus- and minus-strand templates, but does not transcribe subgenomic RNA. Mutations in the 3' conserved sequence element and poly(A) tail of the plus-strand template prevent nsP4-mediated de novo initiation of minus-strand RNA synthesis. nsP4-dependent terminal addition of nucleotides occurs on template RNA possessing certain mutations in the 3' conserved sequence element and polyadenylate tail. nsP4 is capable of minus-strand synthesis independent of the sequence at the 5' end of the template. An A-U rich sequence in the 3' conserved sequence element represents a binding site for a replicase component. Probably nsP4 plus-strand genomic RNA synthesis is dependent on the 3' end of the minus-strand template