3.6.4.13: RNA helicase
This is an abbreviated version!
For detailed information about RNA helicase, go to the full flat file.
Word Map on EC 3.6.4.13
-
3.6.4.13
-
single-stranded
-
strand
-
viruses
-
duplex
-
fork
-
retinoic
-
nucleic
-
chromatin
-
acid-inducible
-
mda5
-
dsrnas
-
ssdna
-
rna-binding
-
stall
-
werner
-
nonstructural
-
bloom
-
polyproteins
-
dna-dependent
-
primase
-
exonuclease
-
replisome
-
spliceosome
-
hexameric
-
minichromosome
-
differentiation-associated
-
dengue
-
g-quadruplexes
-
eif4g
-
single-molecule
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unwound
-
replicase
-
restart
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ifn-stimulated
-
nonsense-mediated
-
rpa
-
rad51
-
holliday
-
polyi:c
-
flavivirus
-
tfiih
-
exoribonuclease
-
ifn-beta
-
d-loops
-
pigmentosum
-
cap-dependent
-
xeroderma
-
positive-stranded
-
pre-rrnas
-
overhang
-
pharmacology
-
medicine
-
drug development
- 3.6.4.13
-
single-stranded
- strand
- viruses
- duplex
- fork
-
retinoic
- nucleic
- chromatin
-
acid-inducible
- mda5
- dsrnas
- ssdna
-
rna-binding
-
stall
-
werner
-
nonstructural
-
bloom
- polyproteins
-
dna-dependent
- primase
-
exonuclease
- replisome
-
spliceosome
-
hexameric
-
minichromosome
-
differentiation-associated
- dengue
-
g-quadruplexes
- eif4g
-
single-molecule
-
unwound
-
replicase
-
restart
-
ifn-stimulated
-
nonsense-mediated
- rpa
- rad51
-
holliday
-
polyi:c
- flavivirus
- tfiih
- exoribonuclease
-
ifn-beta
-
d-loops
- pigmentosum
-
cap-dependent
- xeroderma
-
positive-stranded
- pre-rrnas
-
overhang
- pharmacology
- medicine
- drug development
Reaction
Synonyms
1a NTPase/helicase, Aquarius, AtHELPS, ATP-dependent helicase, ATP-dependent RNA helicase, ATP-dependent RNA helicase DDX3X, ATP-dependent RNA helicase DDX5, ATP/dATP-dependent RNA helicase, ATPase, ATPase/helicase, ATPase/RNA helicase, AtRH3, AtRH7, bel, BmL3-helicase, BMV 1a protein, BRR2, Brr2 RNA helicase, Brr2p, Cbu_0670, ChlR1 helicase, cold-shock DEAD-box protein A, CrhR, CsdA, CshA, CTHT_0005780, CTHT_0009470, DBP2, DbpA, DDX17, DDX19, DDX19B, DDX21, DDX21 RNA helicase, DDX25, DDX27, DDX3, DDX3X, DDX3Y, DDX4, DDX5, DDX58, DeaD, DEAD box helicase, DEAD box RNA helicase, DEAD-box ATP-dependent RNA helicase CshA, DEAD-box helicase, DEAD-box protein DED1, DEAD-box RNA helicase, DEAD-box rRNA helicase, DEAH box protein 34, DEAH-box protein 2, DEAH-box RNA helicase, DEAH/RHA RNA helicase, DED1, DENV NS3H, DEx(H/D)RNA helicase, DExD/H box RNA helicase, DEXD/H-box RNA helicase, dexh helicase, DExH protein RNA helicase A, DExH/D-Box protein RNA helicase A, DExH/D-box RNA helicase, DHX34, DHX36, DHX8, DHX9, Dhx9/RNA helicase A, DNA/RNA-dependent ATPase, EhDEAD1, EhDEAD1 RNA helicase, eIF4A, eIF4A helicase, eIF4AIII, eukaryotic initiation factor eIF 4A, frequency-interacting RNA helicase, FRH, FRQ-interacting RNA helicase, gonadotropin-regulated testicular RNA helicase, GRTH, GRTH/DDX25, HCV NS3 helicase, HEL-1, helicase, helicase 1, helicase B, helicase/nucleoside triphosphatase, HRpA, IBP160, increased size exclusion limit2, intron-binding protein 160, ISE2, KOKV helicase, Lmo1722, mitochondrial DEAD-box RNA helicase, Mss116p, mtr4, Mtr4p, NA-helicase, non structural protein 3, non-structural 3, non-structural protein 3, non-structural protein 3 protein, nonstructural protein 3, NPH-II, NS3, NS3 ATPase/helicase, NS3 helicase, NS3 NTPase/helicase, NS3 protein, NTPase/helicase, nucleoside 5'-triphosphatase, nucleoside triphosphatase/helicase, nucleoside triphosphatase/RNA helicase and 5'-RNA triphosphatase, NWMN_1985, p54 RNA helicase, p68, p68 RNA helicase, P72, PH1280, pre-mRNA-splicing ATP-dependent RNA helicase 28, protein NS3, Prp28, Prp43, Prp5, RENT1, RH22, RHA, RhlB, RIG-I, Rm62, RNA DEAD-box helicase, RNA helicase, RNA helicase A, RNA helicase Aquarius, RNA helicase BELLE, RNA helicase CrhR, RNA helicase CsdA, RNA helicase CshA, RNA helicase DDX17, RNA helicase DDX27, RNA helicase DDX3, RNA helicase Ddx39, RNA helicase DDX3X, RNA helicase DDX5, RNA helicase DDX6, RNA helicase DeaD, RNA helicase DHX34, RNA helicase DHX8, RNA helicase DHX9, RNA helicase HEL-1, RNA helicase Hera, RNA helicase ISE2, RNA Helicase p68, RNA helicase RHAU, RNA helicase UPF1, RNA splicing effector, RNA-dependent ATPase, RNA-dependent NTPase/helicase, RNA-helicase, RTPase, SA1885, Ski2-like helicase, slr0083, SNRNP200, spliceosomal DEAH-box RNA helicase, spliceosomal RNA helicase, SpolvlgA, Supv3L1, TaRH1, TGBp1 NTPase/helicase domain, Tk-DeaD, Triticum aestivum RNA helicase, Upf1, UPF1_1, UPF1_2, Vasa, VRH1, YxiN, ZmRH3, ZmRH3A, ZmRH3B
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3.6.4.13 RNA helicaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.6.4.13 - RNA helicase
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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
2',3'-dideoxy-ATP + H2O
2',3'-dideoxy-ADP + phosphate
-
53% of the phosphohydrolase activity with ATP
-
-
?
2',3'-dideoxy-GTP + H2O
2',3'-dideoxy-GDP + phosphate
-
28% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-ATP + H2O
2'-deoxy-ADP + phosphate
-
62% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-GTP + H2O
2'-deoxy-GDP + phosphate
-
39% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-L-GTP + H2O
2'-deoxy-L-GDP + phosphate
-
11% of the phosphohydrolase activity with ATP
-
-
?
2'-fluoro-2'-deoxy-ATP + H2O
2'-fluoro-2'-deoxy-ADP + phosphate
-
63% of the phosphohydrolase activity with ATP
-
-
?
2'-fluoro-2'-deoxy-GTP + H2O
2'-fluoro-2'-deoxy-GDP + phosphate
-
22% of the phosphohydrolase activity with ATP
-
-
?
2'-O-methyl-GTP + H2O
2'-O-methyl-GDP + phosphate
-
24% of the phosphohydrolase activity with ATP
-
-
?
2-amino-ATP + H2O
2-amino-ADP + phosphate
-
103% of the phosphohydrolase activity with ATP
-
-
?
2-hydroxy-ATP + H2O
2-hydroxy-ADP + phosphate
-
40% of the phosphohydrolase activity with ATP
-
-
?
3'-deoxy-ATP + H2O
3'-deoxy-ADP + phosphate
-
60% of the phosphohydrolase activity with ATP
-
-
?
3'-deoxy-GTP + H2O
3'-deoxy-GDP + phosphate
-
12% of the phosphohydrolase activity with ATP
-
-
?
3'-O-methyl-GTP + H2O
3'-O-methyl-GDP + phosphate
-
35% of the phosphohydrolase activity with ATP
-
-
?
6-methyl-thio-GTP + H2O
6-methyl-thio-GDP + phosphate
-
40% of the phosphohydrolase activity with ATP
-
-
?
6-methyl-thio-ITP + H2O
6-methyl-thio-IDP + phosphate
-
16% of the phosphohydrolase activity with ATP
-
-
?
6-thio-GTP + H2O
6-thio-GDP + phosphate
-
93% of the phosphohydrolase activity with ATP
-
-
?
7-methyl-GTP + H2O
7-methyl-GDP + phosphate
-
14% of the phosphohydrolase activity with ATP
-
-
?
8-bromo-ATP + H2O
8-bromo-ADP + phosphate
-
124% of the phosphohydrolase activity with ATP
-
-
?
8-bromo-GTP + H2O
8-bromo-GDP + phosphate
-
19% of the phosphohydrolase activity with ATP
-
-
?
8-iodo-GTP + H2O
8-iodo-GDP + phosphate
-
54% of the phosphohydrolase activity with ATP
-
-
?
ara-ATP + H2O
ara-ADP + phosphate
-
18% of the phosphohydrolase activity with ATP
-
-
?
dCTP + H2O
dCDP + phosphate
helicase activity is about 25% of the activity with ATP
-
-
?
dGTP + H2O
dGDP + phosphate
helicase activity is about 10% of the activity with ATP
-
-
?
dTTP + H2O
dTDP + phosphate
helicase activity is about 55% of the activity with ATP
-
-
?
ITP + H2O
IDP + phosphate
-
49% of the phosphohydrolase activity with ATP
-
-
?
N1-methyl-ATP + H2O
N1-methyl-ADP + phosphate
-
66% of the phosphohydrolase activity with ATP
-
-
?
N1-methyl-GTP + H2O
N1-methyl-GDP + phosphate
-
49% of the phosphohydrolase activity with ATP
-
-
?
N6-methyl-ATP + H2O
N6-methyl-ADP + phosphate
-
43% of the phosphohydrolase activity with ATP
-
-
?
O6-methyl-GTP + H2O
O6-methyl-GDP + phosphate
-
17% of the phosphohydrolase activity with ATP
-
-
?
ribavirin triphosphate + H2O
ribavirin diphosphate + phosphate
-
36% of the phosphohydrolase activity with ATP
-
-
?
XTP + H2O
XDP + phosphate
-
40% of the phosphohydrolase activity with ATP
-
-
?
ATP + H2O
ADP + phosphate
-
cooperative binding of ATP and RNA leads to a compact helicase structure
-
-
?
ATP + H2O
ADP + phosphate
EF409381
either ATP or dATP is required for the unwinding activity
-
-
?
ATP + H2O
ADP + phosphate
helicase activity requires the substrates possessing a 3' un-base-paired region on the RNA template strand. The NS3h helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of the RNA substrates. CSFV NS3 helicase activity requires a longer 3'-end single-stranded overhang for efficient duplex unwinding and the directionality of NS3 helicase unwinding is 3' to 5' with respect to the template strand
-
-
?
ATP + H2O
ADP + phosphate
-
ATPase activity, ATP binding mode, the ATP binding site is housed between these two subdomains. In the ATP binding pocket, a Mg ion is coordinated in a octahedral manner by the beta- and gamma-phosphate oxygen atoms from ATP, two equatorial water molecules and oxygen atoms from residues Glu285 in motif II, and Thr200 in motif I, overview
-
-
?
ATP + H2O
ADP + phosphate
-
NS3 C-terminal domain catalyzes ATP hydrolysis in the presence of MgCl2 or MnCl2. MgCl2 is more effective than MnCl2 at inducing ATPase activity at concentrations ranging from 0.1 mM to 5 mM. ATP hydrolysis is required for the unwinding activity of DENV NS3H
-
-
?
ATP + H2O
ADP + phosphate
-
wild-type and mutant, NTPase activity analyzed, functional binding of RNA analyzed
-
-
?
ATP + H2O
ADP + phosphate
-
NS3 C-terminal domain catalyzes ATP hydrolysis in the presence of MgCl2 or MnCl2. MgCl2 is more effective than MnCl2 at inducing ATPase activity at concentrations ranging from 0.1 mM to 5 mM. ATP hydrolysis is required for the unwinding activity of DENV NS3H
-
-
?
ATP + H2O
ADP + phosphate
-
wild-type and mutant, NTPase activity analyzed, functional binding of RNA analyzed
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant EhDEAD1 protein presents ATPase activity and is able to bind and unwind RNA in an ATPase-dependent manner
-
-
?
ATP + H2O
ADP + phosphate
-
the 3' to 5' helicase activity of DbpA can use a 3' single-stranded loading site on either strand of the substrate helix
-
-
?
ATP + H2O
ADP + phosphate
the ATP hydrolysis activity of the extended and wild-type DbpA are measured by the pyruvate kinase/lactate dehydrogenase coupled assay. The peptide extension is not effecting the formation of the proper ATP pocket
-
-
?
ATP + H2O
ADP + phosphate
-
the C-terminal portion of hepatitis C virus nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3 to 5 direction. Driven by the energy of ATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA
-
-
?
ATP + H2O
ADP + phosphate
-
the protein binds RNA and DNA in a sequence specific manner. ATP hydrolysis is stimulated by some nucleic acid polymers much better than it is stimulated by others. The range is quite dramatic. Poly(G) RNA does not stimulate at any measurable level, and poly(U) RNA (or DNA) stimulates best (up to 50 fold). HCV helicase unwinds a DNA duplex more efficiently than an RNA duplex. ATP binds HCV helicase between two RecA-like domains, causing a conformational change that leads to a decrease in the affinity of the protein for nucleic acids. One strand of RNA binds in a second cleft formed perpendicular to the ATP-binding cleft and its binding leads to stimulation of ATP hydrolysis. RNA and/or ATP binding likely causes rotation of domain 2 of the enzyme relative to domains 1 and 3, and somehow this conformational change allows the protein to move like a motor
-
-
?
ATP + H2O
ADP + phosphate
unwinds RNA in a discontinuous manner, pausing after long apparent steps of unwinding. It is proposed that the large kinetic step size of NS3 unwinding reflects a delayed, periodic release of the separated RNA product strand from a secondary binding site that is located in the NTPase domain (domain II) of NS3
-
-
?
ATP + H2O
ADP + phosphate
-
multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities
-
-
?
ATP + H2O
ADP + phosphate
-
NTPase activity analyzed, ambiguous helicase activity, enzyme capable for unwinding RNA and DNA
-
-
?
ATP + H2O
ADP + phosphate
RNA-stimulated ATPase activities determined, interaction between the replicative component nonstructural protein 3 (NS3) with the nonstructural protein 4A (NS4A)
-
-
?
ATP + H2O
ADP + phosphate
the Arg-rich amino acid motif HCV1487-1500, a fragment of domain 2 NS3 of Hepatitis C virus, as well as the complete domain 2, and domain 2 lacking the flexible loop localized between Val1458 and Thr1476, mediate competitive inhibition of diverse protein kinase C functions, inhibition of rat brain PKC, overview
-
-
?
ATP + H2O
ADP + phosphate
-
peptide inhibitors derived from amino acid sequence of motif VI analyzed, binding of the inhibitory peptides does not interfere with the NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes. GRTH has a negative role on its mRNA stability
-
-
?
ATP + H2O
ADP + phosphate
-
RHA is a coactivator in STAT6-mediated transcription, and this function is dependent on its helicase activity
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
-
RNA helicase A utilizes all hydrolyzable NTPs without preference. RNA helicase A unwinds dsRNA only in a 3' to 5' direction. The enzyme can only translocate on RNA possessing 3 single-stranded regions
-
-
?
ATP + H2O
ADP + phosphate
-
the enzyme displaces partial duplex RNA exclusively in a 5' to 3' direction. This reaction is supported by ATP and dATP at relatively high concentrations. The enzyme displays only ATPase and dATPase activity. RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
-
-
?
ATP + H2O
ADP + phosphate
enzyme ChlR1 fails to unwind the triplex substrate in the absence of ATP or in the presence of ADP or ATPgammaS
-
-
?
ATP + H2O
ADP + phosphate
importance of the beta-phosphate for nucleotide binding
-
-
?
ATP + H2O
ADP + phosphate
the enzyme has both RNA and DNA duplex-unwinding activities with 5'-to-3' polarity
-
-
?
ATP + H2O
ADP + phosphate
-
translation of HIV-1 gag mRNA is reliant on the ATP-dependent helicase activity of RNA helicase A
-
-
?
ATP + H2O
ADP + phosphate
genome structure, crystals and three-dimensional structure determined, structure of NTP-binding region, conserved residues within the NTP-binding pocket, ATPase and RNA helicase activities determined
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
eIF4A may interact directly with double-stranded RNA, and recognition of helicase substrates occurs via chemical and/or structural features of the duplex. The initial rate and amplitude of duplex unwinding by eIF4A is dependent on the overall stability, rather than the length or sequence, of the duplex substrate. eIF4A helicase activity is minimally dependent on the length of the single-stranded region adjacent to the double-stranded region of the substrate. Interestingly, eIF4A is able to unwind blunt-ended duplexes. eIF4A helicase activity is also affected by substitution of 2'-OH (RNA) groups with 2'-H (DNA) or 2'-methoxyethyl groups
-
-
?
ATP + H2O
ADP + phosphate
-
the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinprotein interactions
-
-
?
ATP + H2O
ADP + phosphate
-
the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinprotein interactions
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
Mtr4p can unwind duplex RNA in the presence of ATP and a single-stranded RNA tail in the 3' to 5' direction
-
-
?
ATP + H2O
ADP + phosphate
the DEAD-box protein DED1 has the ability to balance RNA unwinding with a profound strand annealing activity in a highly dynamic fashion
-
-
?
ATP + H2O
ADP + phosphate
ATP and dATP are the preferred nucleotide substrates. In the presence of ATP or dATP Mtr4p unwinds the duplex region of a partial duplex RNA substrate in the 3' to 5' direction. Mtr4p displays a marked preference for binding to poly(A) RNA relative to an oligoribonucleotide of the same length and a random sequence
-
-
?
ATP + H2O
ADP + phosphate
promotes RNA unwinding. The enzyme also catalyzes strand annealing. The balance between unwinding and annealing activities of DED1 depends on the RNA substrate. ADP also modulates the balance between RNA unwinding and strand annealing
-
-
?
ATP + H2O
ADP + phosphate
the Q motif regulates ATP binding and hydrolysis, the affinity of the protein for RNA substrates and the helicase activity. At least three different protein conformations that are associated with free, ADP-bound and ATP-bound forms of the protein
-
-
?
ATP + H2O
ADP + phosphate
-
unwinding activity specific for single-strand paired RNA, does not unwind dsRNAs
-
-
?
ATP + H2O
ADP + phosphate
-
phosphohydrolase and helicase activities of NPH-II are essential for virus replication
-
-
?
ATP + H2O
ADP + phosphate
-
unwinds duplex RNA exclusively in a 3' to 5' direction with respect to the strand to which the enzyme is bound and along which it is presumed to translocate. NTP hydrolysis by RNA bound NPH-II1 drives processive translocation of the protein in a 3 to 5 direction along the RNA strand
-
-
?
ATP + H2O
ADP + phosphate
either ATP or dATP is required for the unwinding activity, VrRH1 catalyzes unwinding of a double-stranded RNA
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no RNA helicase activities
-
-
?
ATP + H2O
ADP + phosphate
-
the West Nile virus RNA helicase uses the energy derived from the hydrolysis of nucleotides to separate complementary strands of RNA
-
-
?
ATP + H2O
ADP + phosphate
-
the amino acids Arg185, Arg202 and Asn417 are critical for phosphohydrolysis
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no RNA helicase activities
-
-
?
CTP + H2O
CDP + phosphate
helicase activity is about 85% of the activity with ATP
-
-
?
dATP + H2O
dADP + phosphate
EF409381
either ATP or dATP is required for the unwinding activity
-
-
?
dATP + H2O
dADP + phosphate
helicase activity is about 10% of the activity with ATP
-
-
?
dATP + H2O
dADP + phosphate
-
the enzyme displaces partial duplex RNA exclusively in a 5' to 3' direction. This reaction is supported by ATP and dATP at relatively high concentrations. The enzyme displays only ATPase and dATPase activity. RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
-
-
?
dATP + H2O
dADP + phosphate
ATP and dATP are the preferred nucleotide substrates. In the presence of ATP or dATP Mtr4p unwinds the duplex region of a partial duplex RNA substrate in the 3' to 5' direction. Mtr4p displays a marked preference for binding to poly(A) RNA relative to an oligoribonucleotide of the same length and a random sequence
-
-
?
dATP + H2O
dADP + phosphate
either ATP or dATP is required for the unwinding activity, VrRH1 catalyzes unwinding of a double-stranded RNA
-
-
?
GTP + H2O
GDP + phosphate
helicase activity is about 55% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
-
49% of the phosphohydrolase activity with ATP
-
-
?
RNA + H2O
?
-
RNA unwinding activity, the enzyme contains two RecA-like domains, opening and closing of the interdomain cleft during RNA unwinding
-
-
?
RNA + H2O
?
-
RNA unwinding activity, substrate is a 154mer of 23S rRNA generated by T7 polymerase from in vitro transcription
-
-
?
RNA + H2O
?
EF409381
helicase/unwinding activity, either ATP or dATP is required for the unwinding activity
-
-
?
RNA + H2O
?
NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview
-
-
?
RNA + H2O
?
NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview
-
-
?
RNA + H2O
?
-
helicase/unwinding activity, ATP hydrolysis is required for the unwinding activity of DENV NS3H
-
-
?
RNA + H2O
?
unwinding helicase activity, NS3 is ahighly basic protein with multiple RNA binding sites
-
-
?
UTP + H2O
UDP + phosphate
helicase activity is about 55% of the activity with ATP
-
-
?
additional information
?
-
-
using yeast two-hybrid and pull-down assays it is shown that RH22 interacts with the 50S ribosomal protein RPL24
-
-
?
additional information
?
-
ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
-
-
-
additional information
?
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ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
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additional information
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ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
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additional information
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open helicase conformation in the absence of nucleotides, or in the presence of ATP, or ADP, or RNA. In the presence of ADP and RNA, the open conformation is retained. By contrast, cooperative binding of ATP and RNA leads to a compact helicase structure, direct transitions between open and closed conformations, overview
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additional information
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BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell, recruits the other RNA replication factor 2apol and induces 50- to 70-nm membrane invaginations serving as RNA replication compartments, BMV 1a protein also recruits viral replication templates such as genomic RNA3 depending on the BMV 1a protein helicase motif, in absence of 2apol, BMV 1a protein highly stabilizes RNA3 by transferring it to a membrane-associated, nuclease-resistant state, overview
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additional information
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multifunctional enzyme showing protease, helicase, and NTPase activities, the enzyme has a function in RNA replication complex assembly besides its function in RNA synthesis/capping, the enzyme activity is located in the C-terminal nucleoside triphosphatase/helicase domain of the BMV 1a protein RNA replication factor
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additional information
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DEAD box proteins are putative RNA unwinding proteins, BmL3-helicase also is a DEAD box RNA helicase
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additional information
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EF409381
DEAD box proteins are putative RNA unwinding proteins, BmL3-helicase also is a DEAD box RNA helicase
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additional information
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nonstructural protein 3 (NS3) possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus
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additional information
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nonstructural protein 3 (NS3) possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus
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additional information
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NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
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additional information
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NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
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additional information
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NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
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additional information
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the enzyme plays an important role in viral replication
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additional information
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multifunctional enzyme showing protease, helicase, and NTPase activities
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The NS3 protein physically associates with the NS5 polymerase, NS3 andNS5 carry out all the enzymatic activities needed for polyprotein processing and genome replication. NS3 possesses an ATPase/helicase and RNA triphosphatase at its C-terminal end that are essential for RNA replication. In addition to its known enzymatic functions, the NS3 protein appears to be involved in the assembly of an infectious flaviviral particle, through its interactions with NS2A and presumably host cell proteins
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conformational changes during ATP hydrolysis and RNA unwinding: on ssRNA binding, the NS3 enzyme switches to a catalytic competent state imparted by an inward movement of the P-loop, interdomain closure and a change in the divalent metal coordination shell, providing a structural basis for RNA-stimulated ATP hydrolysis. Determination of enzyme structure-function relationship of enzyme bound to single-stranded RNA, to an ATP analogue, to a transition-state analogue and to ATP hydrolysis products. RNA recognition appears largely sequence independent, reaction mechanism and RNA recognition, overview. RNA-unwinding mechanism, overview
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the C-terminal region of NS3 forms the RNA helicase domain, an ATP-driven molecular motor
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additional information
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the helicase domain of Dengue virus NS3 protein, i.e. DENV NS3H, contains RNA-stimulated nucleoside triphosphatase, NTPase, ATPase/helicase, and RNA 5'-triphosphatase, RTPase, activities that are essential for viral RNA replication and capping. A 5'-tailed RNA is a better RTPase substrate than an RNA containing no 5'-dangling nucleotide
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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the helicase domain of Dengue virus NS3 protein, i.e. DENV NS3H, contains RNA-stimulated nucleoside triphosphatase, NTPase, ATPase/helicase, and RNA 5'-triphosphatase, RTPase, activities that are essential for viral RNA replication and capping. A 5'-tailed RNA is a better RTPase substrate than an RNA containing no 5'-dangling nucleotide
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additional information
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nonstructural proteins NS3 and NS5 form complexes in infected mammalian cells
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additional information
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substrate specificity, bifunctional enzyme, NS3 is an RNA-stimulated nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase, overview, the full-length NS3 with or without NS2B cofactor domain exhibits a catalytically more efficient RNA helicase activity than the N-terminally-truncated NS3 helicase domain, suggesting that the protease domain enhances RNA helicase activity
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additional information
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helicase B, RhlB, is one of the five DEAD box RNA-dependent ATPases in Escherichia coli. ATPases found in Escherichia coli. RhlB requires an interaction with the partner protein RNase E for appreciable ATPase and RNA unwinding activities
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RhlB is the only Escherichia coli DEAD box protein that requires a protein partner to stimulate its ATPase activity
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analysis of ATPase and unwinding activities of CsdA_564 and CsdA_1-445, and of RNA-binding properties of the C-terminal regions of CsdA and CsdA_RNA-binding domain, overview
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additional information
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the helicase activity of wild-type DbpA and the extended DbpA is investigated by measuring the unwinding of the 5'-32P labeled 9-mer annealed to the unlabeled 32-mer RNA, 32-mer RNA-DNA or the RNA-PEG chimera. DbpA performs RNA structural isomerizations in the ribosome. The only requirement for a double-helix to serve as a DbpA substrate is for the double-helix to be positioned within the catalytic core's grasp. The RecA-like domains of the DEAD-box proteins, which form their catalytic core, attack one strand of the RNA double-helix and bend it. The bending process forces the release of the complementary RNA strand. The ATP-binding to the RecA-like domains provides the energy for the single-stranded RNA bending, while the ATP hydrolysis causes the release of the second strand of the double-helix from the catalytic core and the regeneration of the enzymes. The extension of the interdomain linker region has no effect on the ability of DbpA to perform its helicase function. Thus, the physical connection of DbpA RNA binding domain to the catalytic core is unimportant for the helicase activity of DbpA, suggesting the DbpA protein is a region-specific enzyme, which would unwind any double-helix substrate near hairpin 92
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additional information
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the multifunctional enzyme shows RNA-dependent NTPase and helicase activities, no activity with ADP and AMP
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additional information
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the mature NS3 protein comprises 5 domains: the N-terminal 2 domains form the serine protease along with the NS4A cofactor, and the C-terminal 3 domains form the helicase. The helicase portion of NS3 can be separated form the protease portion by cleaving a linker. Since the protease portion is more hydrophobic, removing it allows the NS3 helicase fragment to be expressed as a more soluble protein at higher levels in Escherichia coli. The fragment of NS3 possessing helicase activity is referred to as HCV helicase
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additional information
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the C-terminal region of NS3 exhibits RNA-stimulated NTPase, e.g. ATPase, and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by the C-terminal region, NS4A mutants that are defective in ATP-coupled RNA binding are lethal in vivo
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additional information
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the C-terminal region of NS3 exhibits RNA-stimulated NTPase, e.g. ATPase, and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by the C-terminal region, NS4A mutants that are defective in ATP-coupled RNA binding are lethal in vivo
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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DEAD-Box RNA Helicase DDX3 interacts with DDX5. The protein-protein interaction is increased in the G2/M phase
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additional information
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DEAD-Box RNA Helicase DDX3 interacts with DDX5. The protein-protein interaction is increased in the G2/M phase
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human telomerase RNA interacts with the N-terminal domain of RHAU
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additional information
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p68 interacts with an intronic splicing activator, RNA binding motif protein 4 (RBM4), thereby stimulating tau exon 10 inclusion
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additional information
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recombinant N-terminal, central helicase, and C-terminal domains of RHA are evaluated for their ability to specifically interact with cognate RNAs by in vitro biochemical measurements and mRNA translation assays in cells. Results demonstrate that N-terminal residues confer selective interaction with retroviral and junD target RNAs. Conserved lysine residues in the distal alpha-helix of the double-stranded RNA-binding domains are necessary to engage structural features of retroviral and junD 5'-UTRs
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additional information
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RNA helicase A interacts with La ribonucleoprotein domain family member 6 (LARP6) which recruits RHA to the 5' UTR of collagen mRNAs
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additional information
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ChlR1 robustly unwinds DNA triplex substrates in an ATP-dependent manner requiring an 5'-ssDNA tail, ChlR1 can unwind an intramolecular triplex structure
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additional information
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ChlR1 robustly unwinds DNA triplex substrates in an ATP-dependent manner requiring an 5'-ssDNA tail, ChlR1 can unwind an intramolecular triplex structure
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additional information
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enzyme DDX21 inhibits influenza A virus replication. Enzyme DDX21 most likely binds viral PB1 protein in the cytoplasm, where protein PB1 is probably free of the other polymerase subunits, albeit transiently, before it forms a complex with viral protein PA that is imported into the nucleus
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additional information
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human Upf1 is able to translocate slowly over long single-stranded nucleic acids with a high processivity. Upf1 efficiently translocates through double-stranded structures and protein-bound sequences. The helicase domain of Upf1 is capable of both unwinding double-stranded nucleic acids and translocation on single-stranded nucleic acids over long distances. Upf1 remodels nucleoprotein complexes
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additional information
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human Upf1 is able to translocate slowly over long single-stranded nucleic acids with a high processivity. Upf1 efficiently translocates through double-stranded structures and protein-bound sequences. The helicase domain of Upf1 is capable of both unwinding double-stranded nucleic acids and translocation on single-stranded nucleic acids over long distances. Upf1 remodels nucleoprotein complexes
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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wild-type and mutant enzymes in vitro RNA binding and unwinding or in the cell during HIV-1 production during RNA helicase A-RNA interaction and RNA helicase A-stimulated viral RNA processes, overview
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additional information
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RNA-dependent interactions of DHX34 with UPF3b and the EJC component, MLN51, no interaction with PABP1, with the eukaryotic release factor eRF3, or with the NMD core factor UPF2. Interactions of DHX34 with RNA degradation factors such as the exonuclease XRN1, the exosome component DIS3, and the decapping enzyme DCP1, all of them independently of the presence of RNA. DHX34 interacts with UPF1 directly and preferentially associates with SURF complexes, and promoties UPF1 phosphorylation
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additional information
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RNA-dependent interactions of DHX34 with UPF3b and the EJC component, MLN51, no interaction with PABP1, with the eukaryotic release factor eRF3, or with the NMD core factor UPF2. Interactions of DHX34 with RNA degradation factors such as the exonuclease XRN1, the exosome component DIS3, and the decapping enzyme DCP1, all of them independently of the presence of RNA. DHX34 interacts with UPF1 directly and preferentially associates with SURF complexes, and promoties UPF1 phosphorylation
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additional information
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the enzyme DDX21 binds to the RNA binding domain of viral NS1 protein, specifically to a region comprised of amino acids R37, R38, K41 and R44
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additional information
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the purified recombinant ChlR1 protein is a DNA-dependent ATPase and unwinds partial duplex DNA substrates with a preferred 5' to 3' directionality, triplex DNA is the preferred DNA substrate for ChlR1, analysis of diverse DNA substrates, overview
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additional information
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the purified recombinant ChlR1 protein is a DNA-dependent ATPase and unwinds partial duplex DNA substrates with a preferred 5' to 3' directionality, triplex DNA is the preferred DNA substrate for ChlR1, analysis of diverse DNA substrates, overview
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additional information
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Upf1-HD is a slow translocase compared with other monomeric helicases like UvrD and NS3, but is able to translocate slowly over long single-stranded nucleic acids with a high processivity which exceeds the size of the tested hairpins, overview. Enzyme Upf1 is able to both unwind a long dsRNA of 156 bp and translocate onto ssRNA. Active translocating enzyme Upf1 disrupts protein-nucleic acid interactions. Upf1 remodels nucleoprotein complexes. Substrates are RNADNA hybrids, ssDNA and ssRNA
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additional information
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Upf1-HD is a slow translocase compared with other monomeric helicases like UvrD and NS3, but is able to translocate slowly over long single-stranded nucleic acids with a high processivity which exceeds the size of the tested hairpins, overview. Enzyme Upf1 is able to both unwind a long dsRNA of 156 bp and translocate onto ssRNA. Active translocating enzyme Upf1 disrupts protein-nucleic acid interactions. Upf1 remodels nucleoprotein complexes. Substrates are RNADNA hybrids, ssDNA and ssRNA
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additional information
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wild-type and mutant enzymes in vitro RNA binding and unwinding or in the cell during HIV-1 production during RNA helicase A-RNA interaction and RNA helicase A-stimulated viral RNA processes, overview. Ability of wild-type and mutant RHAs to stimulate the accumulation of HIV-1 mRNAs
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additional information
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enzyme Brr2 catalyzes an ATP-dependent unwinding of the U4/U6 RNA duplex
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additional information
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multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel
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additional information
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multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel
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additional information
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Aquarius exhibits ATPase and RNA-unwinding activity in vitro. Consistently with its possessing a Q motif and thus specifically binding ATP, Aquarius does not hydrolyze GT. Aquarius does not bind a blunt-ended RNA duplex
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additional information
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Aquarius exhibits ATPase and RNA-unwinding activity in vitro. Consistently with its possessing a Q motif and thus specifically binding ATP, Aquarius does not hydrolyze GT. Aquarius does not bind a blunt-ended RNA duplex
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additional information
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Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
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additional information
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Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
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additional information
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DHX8 has an in vitro binding preference for adenine-rich RNA, and RNA binding triggers the release of ADP through significant conformational flexibility in the conserved DEAH-, P-loop and hook-turn motifs. DHX8 makes base-specific contacts with RNA and preferentially binds adenine-rich RNA in vitro, RNA-bound DHX8DELTA547-A6 structure, overview. RNA binding triggers nucleotide release and establish the importance of R620 and both the hook-loop and hook-turn for DHX8 helicase activity, proposing that the hook-turn acts as a gatekeeper to aid correct directional RNA movement through the RNA-binding tunnel. Unwinding activity using an RNA/DNA duplex substrate comprising a 60-mer RNA strand (RNA60) annealed to a 30-mer DNA strand fluorescently labelled on the 30 end (DNA30-ATTO680). DHX8 is an RNA-specific helicase by showing that a poly(dA)10 DNA strand cannot displace Cy5-poly(A)10 from DHX8 in the presence of ADP-AlFx. The displacement of the probe with poly(A)10, poly(C)10, poly(G)10 and poly(U)10 RNA indicates that DHX8 has a preference for binding adenine-rich sequences as the rank ascending order of IC50 values is poly (A)10, poly(U)10, poly(C)10, and poly(G)10. Molecular details of RNA binding to DHX8, the RNA base stack is bookended by the beta-hairpin and the hook-turn hairpin, DHX8 forms RNA base-specific interactions through its OB-fold and RecA1 domains, overview
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additional information
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DHX8 has an in vitro binding preference for adenine-rich RNA, and RNA binding triggers the release of ADP through significant conformational flexibility in the conserved DEAH-, P-loop and hook-turn motifs. DHX8 makes base-specific contacts with RNA and preferentially binds adenine-rich RNA in vitro, RNA-bound DHX8DELTA547-A6 structure, overview. RNA binding triggers nucleotide release and establish the importance of R620 and both the hook-loop and hook-turn for DHX8 helicase activity, proposing that the hook-turn acts as a gatekeeper to aid correct directional RNA movement through the RNA-binding tunnel. Unwinding activity using an RNA/DNA duplex substrate comprising a 60-mer RNA strand (RNA60) annealed to a 30-mer DNA strand fluorescently labelled on the 30 end (DNA30-ATTO680). DHX8 is an RNA-specific helicase by showing that a poly(dA)10 DNA strand cannot displace Cy5-poly(A)10 from DHX8 in the presence of ADP-AlFx. The displacement of the probe with poly(A)10, poly(C)10, poly(G)10 and poly(U)10 RNA indicates that DHX8 has a preference for binding adenine-rich sequences as the rank ascending order of IC50 values is poly (A)10, poly(U)10, poly(C)10, and poly(G)10. Molecular details of RNA binding to DHX8, the RNA base stack is bookended by the beta-hairpin and the hook-turn hairpin, DHX8 forms RNA base-specific interactions through its OB-fold and RecA1 domains, overview
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additional information
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substrate determinants for unwinding activity of the DExH/D-Box protein RNA helicase A, overview. RHA translocates efficiently along the 3' overhang of RNA, but not DNA, with a requirement of covalent continuity. Ribose-phosphate backbone lesions on both strands of the nucleic acids, especially on the 3' overhang of the loading strand, affect RHA unwinding significantly. RHA requires RNA on the 3' overhang which directly or indirectly connects with the duplex region to mediate productive unwinding
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additional information
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the two isoforms of UPF differ in their RNA-binding and catalytic activities, the flexible loop in domain 1B affects the catalytic activity of UPF1 isozymes
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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helicase DDX6 colocalizes with TRIM32 in neural stem cells and neurons and increases the activity of Let-7a. The activation of Let-7a depends on the enzyme's helicase activity
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
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Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
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additional information
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Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview. Recombinant N-terminal His-tagged CshA (gene SA1885, N315 genome) binds to 375-nt sarA mRNA
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview. Recombinant N-terminal His-tagged CshA (gene SA1885, N315 genome) binds to 375-nt sarA mRNA
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview. Recombinant N-terminal His-tagged CshA (gene SA1885, N315 genome) binds to 375-nt sarA mRNA
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview. Recombinant N-terminal His-tagged CshA (gene SA1885, N315 genome) binds to 375-nt sarA mRNA
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview
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additional information
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Thermochaetoides thermophila
RNA loading mechanism of Prp43, and catalytic mechanism, detailed overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of interactions between Prp43 and the U7-RNA and of the ATP-bound enzyme structure. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Prp43 translocates RNA via its Hook-Turn
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Thermochaetoides thermophila CBS 144.50
RNA loading mechanism of Prp43, and catalytic mechanism, detailed overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of interactions between Prp43 and the U7-RNA and of the ATP-bound enzyme structure. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Prp43 translocates RNA via its Hook-Turn
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Thermochaetoides thermophila DSM 1495
RNA loading mechanism of Prp43, and catalytic mechanism, detailed overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of interactions between Prp43 and the U7-RNA and of the ATP-bound enzyme structure. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Prp43 translocates RNA via its Hook-Turn
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Thermochaetoides thermophila IMI 039719
RNA loading mechanism of Prp43, and catalytic mechanism, detailed overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of interactions between Prp43 and the U7-RNA and of the ATP-bound enzyme structure. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Prp43 translocates RNA via its Hook-Turn
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TaRH1-catalysed unwinding of duplex RNA
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ATP-dependent unwinding of duplex RNA in vitro by TaRH1
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain
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additional information
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
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additional information
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain
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additional information
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NS3 includes a protease and a helicase that are essential to virus replication and to RNA capping
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additional information
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NS3 includes a protease and a helicase that are essential to virus replication and to RNA capping
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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