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Information on EC 3.6.4.13 - RNA helicase and Organism(s) Homo sapiens and UniProt Accession P17844

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EC Tree
IUBMB Comments
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3' to 5' polarity , other show 5' to 3' polarity . Some helicases unwind DNA as well as RNA [7,8]. May be identical with EC 3.6.4.12 (DNA helicase).
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Homo sapiens
UNIPROT: P17844
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
helicase, rig-i, rna helicase, eif4a, ddx3x, dead-box rna helicase, ns3 helicase, dead-box helicase, ddx21, rna helicase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP-dependent RNA helicase DDX5
-
DEAD box RNA helicase
-
DEAD-box RNA helicase
-
RNA helicase DDX5
-
RNA Helicase p68
-
ATP-dependent helicase
-
Brr2 RNA helicase
-
Brr2p
-
-
ChlR1 helicase
-
DDX21 RNA helicase
-
DDX3X
DDX3Y
DEAD box RNA helicase
-
DEAD-box RNA helicase
-
DEAH box protein 34
-
DEAH-box protein 2
-
DEAH-box RNA helicase
DEAH/RHA RNA helicase
-
DEXD/H-box RNA helicase
-
DExH protein RNA helicase A
-
-
DExH/D-Box protein RNA helicase A
-
DExH/D-box RNA helicase
-
DHX36
-
-
GRTH/DDX25
-
intron-binding protein 160
-
p54 RNA helicase
-
p68 RNA helicase
-
-
RNA helicase A
RNA helicase Aquarius
-
RNA helicase DDX17
-
RNA helicase DDX3
-
RNA helicase DHX34
-
RNA helicase DHX8
-
RNA helicase RHAU
-
-
RNA helicase UPF1
-
RNA-dependent ATPase
-
RNA-helicase
-
Ski2-like helicase
-
spliceosomal RNA helicase
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (RNA helix unwinding)
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3' to 5' polarity [3], other show 5' to 3' polarity [8]. Some helicases unwind DNA as well as RNA [7,8]. May be identical with EC 3.6.4.12 (DNA helicase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
CTP + H2O
CDP + phosphate
show the reaction diagram
-
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
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
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
-
slight stimulation at 0.05-0.1 M, inhibition at 0.2 M
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-(3,5-dimethoxyphenyl)-N-(7-fluoro-3-methoxyquinoxalin-2-yl)piperazine-1-carboxamide
i.e. supinoxin or RX-5902, intervenes in the phosphorylated p68-beta-catenin signaling pathway by interacting with Tyr593 in SK-MEL-28 (human melanoma), MDA-MB-231 (human metastatic breast cancer), and WI-38 (human normal fetal lung fibroblasts) cell lines
(6Z)-6-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-5-imino-2-propyl-5,6-dihydro-7H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-7-one
-
3-[5-[(Z)-(2-cyclohexyl-5-imino-7-oxo-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid
binds an RNA-binding site inside the N-terminal cassette, mechanism of action, enzyme binding structure, overview
3-[5-[(Z)-(5-imino-7-oxo-2-propyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid
-
6-benzyl-3-[(2R)-2-(3-fluoropyridin-2-yl)-6-methyl-3,4-dihydro-2H-1-benzopyran-7-yl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione
binds to an unexpected allosteric site between the C-terminal and the N-terminal helicase cassettes, enzyme binding structure, overview
6-benzyl-3-[3-(benzyloxy)phenyl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione
enzyme binding structure, overview
ADP
the affinity for RNA is over 90fold weaker in the absence of nucleotide and in the presence of ADP, the RNA affinity is too weak to determine. These results indicate that DHX8-mediated disruption of RNA interactions occurs through a series of alternating strong and weak RNA binding events controlled by ATP hydrolysis. Both full-length fl-DHX8 and truncated DHX8DELAT547 preferentially bind the purine nucleotides ADP and GDP, but are also able to bind CDP, TDP and UDP. RNA binding triggers DEAH and P-loop movement and stimulates ADP release
AMP-PNP
structure of Aquarius in complex with AMP-PNP, modelling, overview
benzoquinoquinoxaline
BQQ, inhibits ChlR1 triplex DNA unwinding activity
EDTA
-
-
EWS-FLI1
the small molecule reduces RHA helicase activity in a dose-dependent and enantiomeric manner without affecting intrinsic ATPase activity, the RHA kinetics indicate a complex model. Only (S)-YK-4-279 reverses the EWS-FLI1 inhibition of RHA helicase activity. YK-4-279 inhibition of RHA binding to EWS-FLI1 alters the RNA binding profile of both proteins. EWS-FLI1 modulates RHA helicase activity causing changes in overall transcriptome processing
-
poly(A)10
-
-
poly(A)4
-
-
poly(A)6
-
-
poly(A)8
-
-
poly(C)10
-
-
poly(G)10
-
-
poly(U)10
-
-
poly(X) RNA
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, poly(G)10
-
Prp8 protein
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MLN51
stimulates the RNA-helicase activity of eIF4AIII
-
poly(C)
-
stimulates ATPase and dATPase activity
Prp8 protein
the Jab1 domain of the Prp8 protein can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved, Brr2-Jab1 binding structure and analysis, overview
-
RNA
Aquarius hydrolyzes ATP, and this activity is highly stimulated in the presence of a 22-nt RNA with a random sequence. Aquarius does not bind a blunt-ended RNA duplex, and correspondingly the latter does not stimulate Aquarius's ATPase activity
Single-stranded RNA
-
RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
ssRNA
DHX8 ATPase activity is stimulated by RNA
-
Upf2
interaction analysis. The two proteins Upf1 and Upf2 form a complex while unwinding RNA. The binding of Upf2 to CH domain activates Upf1-CH-HD unwinding and translocation
-
additional information
Brr2 can be autoinhibited via a large N-terminal region folding back onto its helicase core and autoactivated by a catalytically inactive C-terminal helicase cassette
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0157 - 0.24
ATP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0283 - 0.3
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
(6Z)-6-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-5-imino-2-propyl-5,6-dihydro-7H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-7-one
Homo sapiens
above, pH and temperature not specified in the publication
0.0053
3-[5-[(Z)-(2-cyclohexyl-5-imino-7-oxo-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0042
3-[5-[(Z)-(5-imino-7-oxo-2-propyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0026
ADP
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
0.016
poly(A)10
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
-
0.1
poly(A)4
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
-
0.036
poly(A)6
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
-
0.017
poly(A)8
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
assay at, ATPase assay
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
26
RNA assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
p68 is highly expressed in several carcinomas, such as breast, prostate, and colon
Manually annotated by BRENDA team
fetal lung fibroblasts
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
DDX3 and DDX5 both co-localize in the cytoplasm
Manually annotated by BRENDA team
DDX5 is shutteld into the nucleus by DDX3
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DDX5_HUMAN
614
0
69148
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
x * 100000, gel filtration
119037
x * 119037, calculated from sequence
130000
-
glycerol gradient centrifugation
140000
246000
-
calculated from sequence. Apart from an N-terminal domain of unknown function, Brr2p consists of two putative helicase domains, each connected at its C-terminus to a Sec63-like domain
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 130000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation
phosphoprotein
sumoylation
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation. P68 may be sumoylated on site K53 residue, which may be associated with transcriptional coactivation
ubiquitination
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of RIG-1, PDB ID 2YKG
crystal structure analysis, PDB ID 3G0H
crystals of DDX1954-475 in complex with RNA and Mg/adenosine 5'-(beta,gamma-imido)triphosphate are obtained by vapor diffusion in sitting drops incubated at 4°C by mixing 0.0001 ml of protein solution (20 mg/ml) including 10-molar excess of decauracil ssRNA, adenosine 5'-(beta,gamma-imido)triphosphate, and MgCl2 and 0.0002 ml of reservoir solution containing 14% polyethylene glycol monomethyl ether 2000, 0.25 M trimethylamine n-oxide, 0.1 M Tris, pH 8. The crystal structures of DDX19, in its RNA-bound prehydrolysis and free posthydrolysis state, reveal an alpha-helix that inserts between the conserved domains of the free protein to negatively regulate ATPase activity
hanging-drop method, crystallization of recombinant DDX3 RNA helicase domain
purified recombinant Brr2-Jab1 complex, for complex 1: yBrr2FL and yJab1 are mixed in a 1:2 molar ratio in 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, and separated by gel filtration and and concentrated to 2 mg/ml, followed by sitting drop vapor diffusion technique, mixing of 0.0013 ml of protein solution with 0.0013 ml of reservoir solution containing 0.1 M Tris-HCl, pH 7.5, 10.5% w/v PEG 3350, and 0.2 M MgCl2, 18°C. For complex 2: yBrr2T2, yJab1 and yNtr2 are mixed in a 1:5:5 molar ratio in 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, and separated by gel filtration and and concentrated to 4 mg/ml, followed by hanging drop vapor diffusion technique, mixing of 0.0005 ml of protein solution with 0.00025 ml of reservoit solution containing 0.1 M MES-NaOH, pH 6.5, 9.2% w/v PEG 4000, 0.4 M MgCl2, and with 0.00025 ml 0.33% w/v 1,5-naphthalenedisulfonic acid, 18°C. X-ray diffraction structure determination and analysis at 3.4-4.2 A resolution, molecular replacement using the yBrr2T4-Jab1 structure coordinates as the search model (PDB ID 4BGD)
purified recombinant Brr2-Jab1 complex, X-ray diffraction structure determination and analysis at 3.4-4.2 A resolution
purified recombinant detagged enzyme in complex with inhibitors 6-benzyl-3-[(2R)-2-(3-fluoropyridin-2-yl)-6-methyl-3,4-dihydro-2H-1-benzopyran-7-yl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione, 6-benzyl-3-[3-(benzyloxy)phenyl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione, and 3-[5-[(Z)-(2-cyclohexyl-5-imino-7-oxo-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid, X-ray diffraction structure determination and analysis at 2.75 A, 2.95 A, and 2.80 A resolution, respectivly
purified recombinant enzyme Aquanrius, X-ray diffraction structure determination and analysis at 2.3 A resolution
purified recombinant helicase core of UPF1_1 in its apo-state, X-ray diffraction structure determination and analysis at 3.34 A resolution. Analysis of the X-ray crystal structures of the different states of UPF1_2DELTACH mutant
recombinant catalytic core fragment DHX8DELTA547 bound to ADP and to poly(A)6 single-strand RNA, hanging-drop vapour-diffusion, mixing of 500 nl of protein solution consisting of 3 mg/ml DHX8DELTA547, 1 mM ADP, and 1 mM MgCl2, with 0.00015 ml of reservoir solution comprising 15% v/v 2-methyl-2,4-pentanediol, 100 mM sodium acetate, pH 5.5 and 6% v/v DMSO, and equilibration over 0.25 ml reservoir solution. For the DHX8DELTA547 structure bound to poly(A)6 RNA, a DHX8DELTA547 crystal grown in the presence of ADP is soaked with 1 mM poly(A)6 ssRNA at 4°C for 48 h, X-ray diffraction structure determination and analysis at 2.3-3.2 A resolution, molecular replacement using the structures of RecA1 and RecA2 domains of Saccharomyces cerevisiae Prp43 (PDB ID 2XAU) and of helicase-associated domain of DHX8 (PDB ID 3I4U) as two independent search models
sitting-drop vapor diffusion method at 4 °C. Crystal structures of the conserved domain 1 of the DEIH-motif-containing helicase DHX9 and of the DEAD-box helicase DDX20. Both contain a RecA-like core, but DHX9 differs from DEAD-box proteins in the arrangement of secondary structural elements and is more similar to viral helicases such as NS3. The N-terminus of the DHX9 core contains two long alpha-helices that reside on the surface of the core without contributing to nucleotide binding
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D279A
site-directed mutagenesis, the mutation affects ATP hydrolysis
DELTA53-105
-
a region within the N-terminus of RHAU, referred to as the RSM, interacts with human telomerase RNA
F192E
site-directed mutagenesis, the mutant shows slightly reduced activity compared with the wild-type enzyme. Upf1F192E definitely prefers to unwind a dsDNA than to translocate it, strand switching
K191S
site-directed mutagenesis, the mutation affects ATP binding
K235A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD2, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K236A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD2, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K236E
-
mutant exhibits relatively minor reduction in interaction with SNV PCE
K50R
site-directed mutagenesis, ATPase dead mutant, fails completely to unwind triplex substrates
K54A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD1, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K54A/K55A
-
mutant exhibits relatively minor reduction in interaction with SNV PCE
K54A/K55A/K236E
-
triple mutant shows a severe reduction in interaction with junD post-transcriptional control element (PCE) or SNV PCE compared with wild-type
K55A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD1, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K829A
site-directed mutagenesis, mutation of the invariant lysine residue from motif I involved in ATP binding and hydrolysis drastically reduced Aquarius's ability to bind ATP and ADP and to hydroxadlyze ATP, the mutant shows significantly reduced ATPase activity compared to wild-type enzyme
K897del
site-directed mutagenesis, the mutant fails in unwinding the DNA substrates
Y1196A
site-directed mutagenesis, mutation of a conserved aromatic residue located near the putative RNA-binding surface of the RecA2 inhibits Aquarius's RNA-unwinding activity without changing its RNA-binding and ATPase properties, a helicase-deficient mutant
Y593F
-
expression of the mutant enzyme in SW620 cells leads to Snail repression, E-cadherin upregulation and vimentin repression
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
recombinant C-terminally His-tagged and N-terminally calmodulin-binding-protein-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Rosetta by nickel and calmodulin affinity chromatography
recombinant CBP- and His-tagged wild-type and mutant isozymes from Escherichia coli strain BL21(DE3) by nickel affinity and calmodulin affinity chromatography, followed by dialysis
recombinant His-tagged enzyme by nickel affinity chromatography and anion exchange chromatography
recombinant His-tagged enzyme from Spodoptera frugiperda Sf9 cells by nickel affinity and heparin affinity chromatography
recombinant His10-tagged Brr2 fragments from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration
recombinant His6-GST-tagged full-length DHX8 and truncated mutant DHX8DELTA547 from Sf9 insect cells by nickel affinity and heparin affinity chromatography, and gel filtration
recombinant His6-tagged enzyme from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography, tag cleavage by TEV protease, follwed by dialysis, another step of nickel affinity chromatography, and ultrafiltration of the flow-through
recombinant N-terminally His6-tagged mutant enzymes from HEK293E cells by nickel affinity chromatography
using affinity chromatography
-
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene DDX5, is located in the region 17q23-q25
recombinantly expressed as a His-tagged fusion protein
expressed in Escherichia coli BL-21
-
expression in Escherichia coli
gene BRR2, recombinant expression of His10-tagged TEV-cleavable codon-optimized DNA fragments encoding selected regions of yBrr2 in Escherichia coli strain Rosetta2 (DE3)
gene SNRNP200
gene SNRNP200, recombinant expression of His10-tagged TEV-cleavable codon-optimized DNA fragments encoding selected regions of hBrr2 in Escherichia coli strain Rosetta2 (DE3)
overexpression in Escherichia coli
recombinant expression of C-terminally His-tagged and N-terminally calmodulin-binding-protein-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rosetta
recombinant expression of C-terminally His6-GST-tagged full-length DHX8 (fl-DHX8) and truncated construct containing the complete catalytically active C-terminal helicase core region (DHX8DELTA547) in Spodoptera frugiperda Sf9 cells using the baculovirus expression system
recombinant expression of FLAG-tagged DHX34 in HEK-293T cells, co-expression with recombinant UPF1 protein, DHX34 and UPF1 interact directly, but weak interaction with UPF2 and UPF3b
recombinant expression of FLAG3-tagged wild-type and mutant enzymes in HEK293T cells
recombinant expression of His-tagged enzyme
recombinant expression of N-terminally His6-tagged enzyme in Spodooptera frugiperda Sf9 cells
recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in HEK293e cells
recombinant expression of wild-type and mutant isozymes, that are CBP-tagged at the N-terminus and His-tagged at the C-terminus, in Escherichia coli strain BL21(DE3)
recombinant His-tagged enzyme expression in Spodoptera frugiperda Sf9 cells using the baculovirus expression system
recombinantly expressed as a His-tagged fusion protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an alpha-helix that inserts between the conserved domains of the free protein negatively regulate ATPase activity
polymerase II can interact with beta-actin, and this interaction is enhanced due to the overexpression of RNA helicase A
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
enzyme p68 is a drug target in the treatment of cancer, e.g. breast cancer
medicine
analysis of tumorigenic function of p68 in association with its targeting potential for the treatment of breast cancer
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rodamilans, B.; Montoya, G.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain
Acta Crystallogr. Sect. F
63
283-286
2007
Homo sapiens (O00571), Homo sapiens
Manually annotated by BRENDA team
Abdelhaleem, M.
RNA helicases: regulators of differentiation
Clin. Biochem.
38
499-503
2005
Homo sapiens (O00571), Homo sapiens (O15523), Homo sapiens (Q9NQI0), Homo sapiens (Q9UHL0), Homo sapiens, Mus musculus (Q501J6), Mus musculus (Q61656), Mus musculus (Q9QY15), Rattus norvegicus (Q9QY16)
Manually annotated by BRENDA team
Lee, C.G.; Hurwitz, J.
A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3' to 5' direction.
J. Biol. Chem.
267
4398-4407
1992
Homo sapiens
Manually annotated by BRENDA team
Flores-Rozas, H.; Hurwitz, J.
Characterization of a new RNA helicase from nuclear extracts of HeLa cells which translocates in the 5' to 3' direction.
J. Biol. Chem.
268
21372-21383
1993
Homo sapiens
Manually annotated by BRENDA team
Gutti, R.K.; Tsai-Morris, C.H.; Dufau, M.L.
Gonadotropin-regulated testicular helicase (DDX25), an essential regulator of spermatogenesis, prevents testicular germ cell apoptosis
J. Biol. Chem.
283
17055-17064
2008
Homo sapiens (Q9UHL0)
Manually annotated by BRENDA team
Imamura, O.; Saiki, K.; Tani, T.; Ohshima, Y.; Sugawara, M.; Furuichi. Y.
Cloning and characterization of a human DEAH-box RNA helicase, a functional homolog of fission yeast Cdc28/Prp8
Nucleic Acids Res.
26
2063-2068
1998
Homo sapiens (O60231), Homo sapiens
Manually annotated by BRENDA team
Vlineva, T.; Yang, J.; Silvennoinen, O.
Characterization of RNA helicase A as component of STAT6-dependent enhanceosome
Nucleic Acids Res.
34
3938-3946
2006
Homo sapiens
Manually annotated by BRENDA team
Noble, C.G.; Song, H.
MLN51 stimulates the RNA-helicase activity of eIF4AIII
PLoS One
21
e303
2007
Homo sapiens (P38919)
Manually annotated by BRENDA team
Tang, W.; You, W.; Shi, F.; Qi, T.; Wang, L.; Djouder, Z.; Liu, W.; Zeng, X.
RNA helicase A acts as a bridging factor linking nuclear beta-actin with RNA polymerase II
Biochem. J.
420
421-428
2009
Homo sapiens
Manually annotated by BRENDA team
Hahn, D.; Beggs, J.D.
Brr2p RNA helicase with a split personality: insights into structure and function
Biochem. Soc. Trans.
38
1105-1109
2010
Homo sapiens
Manually annotated by BRENDA team
Collins, R.; Karlberg, T.; Lehtioe, L.; Schuetz, P.; van den Berg, S.; Dahlgren, L.G.; Hammarstroem, M.; Weigelt, J.; Schueler, H.
The DEXD/H-box RNA helicase DDX19 is regulated by an alpha-helical switch
J. Biol. Chem.
284
10296-10300
2009
Homo sapiens (Q9UMR2), Homo sapiens
Manually annotated by BRENDA team
Schuetz, P.; Wahlberg, E.; Karlberg, T.; Hammarstroem, M.; Collins, R.; Flores, A.; Schueler, H.
Crystal structure of human RNA helicase A (DHX9): structural basis for unselective nucleotide base binding in a DEAD-box variant protein
J. Mol. Biol.
400
768-782
2010
Homo sapiens (Q08211), Homo sapiens
Manually annotated by BRENDA team
Minshall, N.; Kress, M.; Weil, D.; Standart, N.
Role of p54 RNA helicase activity and its C-terminal domain in translational repression, P-body localization and assembly
Mol. Biol. Cell
20
2464-2472
2009
Homo sapiens (P26196), Homo sapiens
Manually annotated by BRENDA team
Carter, C.L.; Lin, C.; Liu, C.Y.; Yang, L.; Liu, Z.R.
Phosphorylated p68 RNA helicase activates Snail1 transcription by promoting HDAC1 dissociation from the Snail1 promoter
Oncogene
29
5427-5436
2010
Homo sapiens
Manually annotated by BRENDA team
Ranji, A.; Shkriabai, N.; Kvaratskhelia, M.; Musier-Forsyth, K.; Boris-Lawrie, K.
Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs
J. Biol. Chem.
286
5328-5337
2011
Homo sapiens
Manually annotated by BRENDA team
Choi, Y.J.; Lee, S.G.
The DEAD-box RNA helicase DDX3 interacts with DDX5, co-localizes with it in the cytoplasm during the G2/M phase of the cycle, and affects its shuttling during mRNP export
J. Cell. Biochem.
113
985-996
2012
Homo sapiens, Homo sapiens (P17844)
Manually annotated by BRENDA team
Kar, A.; Fushimi, K.; Zhou, X.; Ray, P.; Shi, C.; Chen, X.; Liu, Z.; Chen, S.; Wu, J.Y.
RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5 splice site
Mol. Cell. Biol.
31
1812-1821
2011
Homo sapiens (P17844)
Manually annotated by BRENDA team
Booy, E.P.; Meier, M.; Okun, N.; Novakowski, S.K.; Xiong, S.; Stetefeld, J.; McKenna, S.A.
The RNA helicase RHAU (DHX36) unwinds a G4-quadruplex in human telomerase RNA and promotes the formation of the P1 helix template boundary
Nucleic Acids Res.
40
4110-4124
2012
Homo sapiens
Manually annotated by BRENDA team
Manojlovic, Z.; Stefanovic, B.
A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs
RNA
18
321-334
2012
Homo sapiens
Manually annotated by BRENDA team
Xing, L.; Niu, M.; Zhao, X.; Kleiman, L.
Different activities of the conserved lysine residues in the double-stranded RNA binding domains of RNA helicase A in vitro and in the cell
Biochim. Biophys. Acta
1840
2234-2243
2014
Homo sapiens (Q08211)
Manually annotated by BRENDA team
Chen, G.; Liu, C.H.; Zhou, L.; Krug, R.M.
Cellular DDX21 RNA helicase inhibits influenza A virus replication but is counteracted by the viral NS1 protein
Cell Host Microbe
15
484-493
2014
Homo sapiens (Q9NR30)
Manually annotated by BRENDA team
Hug, N.; Caceres, J.F.
The RNA helicase DHX34 activates NMD by promoting a transition from the surveillance to the decay-inducing complex
Cell Rep.
8
1845-1856
2014
Homo sapiens (Q14147), Homo sapiens
Manually annotated by BRENDA team
Leitao, A.L.; Costa, M.C.; Enguita, F.J.
Unzippers, resolvers and sensors: a structural and functional biochemistry tale of RNA helicases
Int. J. Mol. Sci.
16
2269-2293
2015
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P21372), Saccharomyces cerevisiae (P47047), Dengue virus, Hepacivirus C, Neurospora crassa, Yellow fever virus, Homo sapiens (O95786), Homo sapiens (Q9UMR2), Murray Valley encephalitis virus (P05769), Kunjin virus (P14335), Japanese encephalitis virus (P27395)
Manually annotated by BRENDA team
Guo, M.; Hundseth, K.; Ding, H.; Vidhyasagar, V.; Inoue, A.; Nguyen, C.H.; Zain, R.; Lee, J.S.; Wu, Y.
A distinct triplex DNA unwinding activity of ChlR1 helicase
J. Biol. Chem.
290
5174-5189
2015
Homo sapiens (Q96FC9), Homo sapiens
Manually annotated by BRENDA team
Fiorini, F.; Bagchi, D.; Le Hir, H.; Croquette, V.
Human Upf1 is a highly processive RNA helicase and translocase with RNP remodelling activities
Nat. Commun.
6
7581
2015
Homo sapiens (Q92900), Homo sapiens
Manually annotated by BRENDA team
Erkizan, H.V.; Schneider, J.A.; Sajwan, K.; Graham, G.T.; Griffin, B.; Chasovskikh, S.; Youbi, S.E.; Kallarakal, A.; Chruszcz, M.; Padmanabhan, R.; Casey, J.L.; Ueren, A.; Toretsky, J.A.
RNA helicase A activity is inhibited by oncogenic transcription factor EWS-FLI1
Nucleic Acids Res.
43
1069-1080
2015
Homo sapiens (Q08211)
Manually annotated by BRENDA team
Felisberto-Rodrigues, C.; Thomas, J.C.; McAndrew, C.; Le Bihan, Y.V.; Burke, R.; Workman, P.; van Montfort, R.L.M.
Structural and functional characterisation of human RNA helicase DHX8 provides insights into the mechanism of RNA-stimulated ADP release
Biochem. J.
476
2521-2543
2019
Homo sapiens (Q14562), Homo sapiens
Manually annotated by BRENDA team
Xie, Q.; Liu, J.; Shan, Y.; Wang, S.; Liu, F.
Substrate determinants for unwinding activity of the DExH/D-Box protein RNA helicase A
Biochemistry
57
6662-6668
2018
Homo sapiens (Q08211)
Manually annotated by BRENDA team
Giraud, G.; Terrone, S.; Bourgeois, C.F.
Functions of DEAD box RNA helicases DDX5 and DDX17 in chromatin organization and transcriptional regulation
BMB Rep.
51
613-622
2018
Drosophila melanogaster, Drosophila melanogaster (P19109), Homo sapiens (P17844), Homo sapiens (Q92841), Mus musculus (Q501J6), Mus musculus (Q61656)
Manually annotated by BRENDA team
Absmeier, E.; Santos, K.F.; Wahl, M.C.
Functions and regulation of the Brr2 RNA helicase during splicing
Cell Cycle
15
3362-3377
2016
Homo sapiens (O75643), Homo sapiens, Saccharomyces cerevisiae (P32639), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P32639)
Manually annotated by BRENDA team
Absmeier, E.; Becke, C.; Wollenhaupt, J.; Santos, K.F.; Wahl, M.C.
Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2
Cell Cycle
16
100-112
2017
Thermochaetoides thermophila (G0S0B9), Homo sapiens (O75643), Thermochaetoides thermophila IMI 039719 (G0S0B9), Thermochaetoides thermophila DSM 1495 (G0S0B9), Thermochaetoides thermophila CBS 144.50 (G0S0B9)
Manually annotated by BRENDA team
Hashemi, V.; Masjedi, A.; Hazhir-Karzar, B.; Tanomand, A.; Shotorbani, S.S.; Hojjat-Farsangi, M.; Ghalamfarsa, G.; Azizi, G.; Anvari, E.; Baradaran, B.; Jadidi-Niaragh, F.
The role of DEAD-box RNA helicase p68 (DDX5) in the development and treatment of breast cancer
J. Cell. Physiol.
234
5478-5487
2019
Homo sapiens (P17844), Homo sapiens
Manually annotated by BRENDA team
Iwatani-Yoshihara, M.; Ito, M.; Klein, M.G.; Yamamoto, T.; Yonemori, K.; Tanaka, T.; Miwa, M.; Morishita, D.; Endo, S.; Tjhen, R.; Qin, L.; Nakanishi, A.; Maezaki, H.; Kawamoto, T.
Discovery of allosteric inhibitors targeting the spliceosomal RNA helicase Brr2
J. Med. Chem.
60
5759-5771
2017
Homo sapiens (O75643)
Manually annotated by BRENDA team
De, I.; Bessonov, S.; Hofele, R.; dos Santos, K.; Will, C.L.; Urlaub, H.; Luehrmann, R.; Pena, V.
The RNA helicase Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes
Nat. Struct. Mol. Biol.
22
138-144
2015
Homo sapiens (O60306), Homo sapiens
Manually annotated by BRENDA team
Gowravaram, M.; Bonneau, F.; Kanaan, J.; Maciej, V.D.; Fiorini, F.; Raj, S.; Croquette, V.; Le Hir, H.; Chakrabarti, S.
A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner
Nucleic Acids Res.
46
2648-2659
2018
Homo sapiens (Q92900)
Manually annotated by BRENDA team