although the the enzyme unwinds the 3'-protruded helix in an ATP-dependent manner, it unwinds the 5'-protruded helix exactly like an RNA chaperone, which is able to unwind the helix in the absence of ATP, and increasing ATP concentrations cannot further enhance the helix unwinding
purified recombinant AtRH57-His protein unwinds double-stranded RNA independently of ATP in vitro, the enzyme AtRH57 might be an ATP-independent RNA helicase
purified recombinant AtRH57-His protein unwinds double-stranded RNA independently of ATP in vitro, the enzyme AtRH57 might be an ATP-independent RNA helicase
purified recombinant AtRH57-His protein unwinds double-stranded RNA independently of ATP in vitro, the enzyme AtRH57 might be an ATP-independent RNA helicase
the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
enzyme DENV NS3 contains ATP-dependent RNA helicase activity and ATP-independent RNA strand annealing activity, it establishes an ATP-dependent steady-state between RNA unwinding and strand annealing
enzyme DENV NS3 contains ATP-dependent RNA helicase activity and ATP-independent RNA strand annealing activity, it establishes an ATP-dependent steady-state between RNA unwinding and strand annealing
the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
enzyme DENV NS3 contains ATP-dependent RNA helicase activity and ATP-independent RNA strand annealing activity, it establishes an ATP-dependent steady-state between RNA unwinding and strand annealing
the enzyme functions not only as an RNA helicase that 3'-to-5' unwinds RNA and DNA helices in an ATP-dependent manner, but also as an RNA chaperone that destabilizes helices bidirectionally and facilitates strand annealing and complex RNA structure formation independently of ATP
the enzyme has both ATP-dependent RNA helicase activity that unwinds RNA helices from both 5'->3' and 3'->5' directions and ATP-independent RNA-chaperoning activity that can remodel structured RNAs and facilitate strand annealing. Moreover, the enzyme can facilitate viral RNA synthesis in vitro by norovirus polymerase
the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
the enzyme requires the presence of Mg2+ to reach its optimal unwinding activity, it is still able to unwind a portion of the RNA helix in the absence of Mg2+ or any divalent ions
guanidine hydrochloride inhibits the ATPase activity of the enzyme in a dose-dependent manner, while the addition of guanidine hydrochloride has no obvious effect on enzyme RNA-chaperoning activity
viral ATPases, including NS3 from flaviviruses, are stimulated by single-stranded RNA. At RNA saturation, an increase of 13.5fold and 9.6fold is achieved with respect to the basal activities for recombinant mutant NS3-FL and NS3-hel, respectively
enzyme AtRH57 belongs to class II DEAD-box RNA helicase gene family. AtRH57 contains a DESD sequence in motif II and is thus classified into the DExD group
enzyme AtRH57 belongs to class II DEAD-box RNA helicase gene family. AtRH57 contains a DESD sequence in motif II and is thus classified into the DExD group
Arabidopsis thaliana T-DNA insertion mutant rh57-1 exhibits hypersensitivity to glucose and abscisic acid. The other two rh57 mutants also show glucose hypersensitivity similar to rh57-1, strongly suggesting that the Glc-hypersensitive feature of these mutants results from mutation of AtRH57. Mutants rh57-1 and rh57-3 display severely impaired seedling growth when grown in Glc concentrations higher than 3%. Transcripts of Glc-responsive genes are altered in rh57 mutants, rh57 mutants exhibit abscisic acid hypersensitivity and enhanced abscisic acid accumulation by Glc. Decreased processing of pre-rRNA products in rh57 mutants. rh57-1 mutants show resistance to antibiotics, e.g. streptomycin. Phenotypes, overview
Arabidopsis thaliana T-DNA insertion mutant rh57-1 exhibits hypersensitivity to glucose and abscisic acid. The other two rh57 mutants also show glucose hypersensitivity similar to rh57-1, strongly suggesting that the Glc-hypersensitive feature of these mutants results from mutation of AtRH57. Mutants rh57-1 and rh57-3 display severely impaired seedling growth when grown in Glc concentrations higher than 3%. Transcripts of Glc-responsive genes are altered in rh57 mutants, rh57 mutants exhibit abscisic acid hypersensitivity and enhanced abscisic acid accumulation by Glc. Decreased processing of pre-rRNA products in rh57 mutants. rh57-1 mutants show resistance to antibiotics, e.g. streptomycin. Phenotypes, overview
the enzyme is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner
the enzyme is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner
the participation of enzyme NS3, modulating the folding of cis-acting RNA elements by the dual RNA unwinding/annealing activities, provides an additional biological role for this viral protein
the participation of enzyme NS3, modulating the folding of cis-acting RNA elements by the dual RNA unwinding/annealing activities, provides an additional biological role for this viral protein
the enzyme NS3 contains the viral serine protease at the N-terminus and ATPase, RTPase, and helicase activities at the C-terminus. Although the helicase domain, comprising amino acids 171 to 618, is an active enzyme, the protease domain has been proposed to have a modulatory role on the helicase and NTPase activities. RNA binding induces a conformational change in the NS3 to a closed form, while no changes in protein structure are observed in different nucleotide-bound states
the enzyme NS3 contains the viral serine protease at the N-terminus and ATPase, RTPase, and helicase activities at the C-terminus. Although the helicase domain, comprising amino acids 171 to 618, is an active enzyme, the protease domain has been proposed to have a modulatory role on the helicase and NTPase activities. RNA binding induces a conformational change in the NS3 to a closed form, while no changes in protein structure are observed in different nucleotide-bound states
the enzyme NS3 contains the viral serine protease at the N-terminus and ATPase, RTPase, and helicase activities at the C-terminus. Although the helicase domain, comprising amino acids 171 to 618, is an active enzyme, the protease domain has been proposed to have a modulatory role on the helicase and NTPase activities. RNA binding induces a conformational change in the NS3 to a closed form, while no changes in protein structure are observed in different nucleotide-bound states
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of crystal structures of the full-length NS3 from Dengue virus and Hepatitis C virus indicates a major difference in the relative orientations between the protease and helicase domains in the two proteins. Specifically, a beta-strand in the HCV NS3 clamps the protease domain next to the helicase domain, thereby creating a compact conformational state that differs from the extended conformation observed in the DENV protein
site-directed mutagenesis, inactive mutant showing no ATP hydrolysis. A mutant NS3-hel carrying a two amino acid substitution (D284A-E285A) in the conserved motif II, which corresponds to the Mg2+ co-factor binding loop
site-directed mutagenesis, inactive mutant showing no ATP hydrolysis. A mutant NS3-hel carrying a two amino acid substitution (D284A-E285A) in the conserved motif II, which corresponds to the Mg2+ co-factor binding loop
construction of enzyme-deficient mutant rh57-1, the mutant is affected in the glucose metabolism and shows reduced function of protein synthesis, rh57-1 mutants show resistance to antibiotics, phenotypes, overview
construction of enzyme-deficient mutant rh57-1, the mutant is affected in the glucose metabolism and shows reduced function of protein synthesis, rh57-1 mutants show resistance to antibiotics, phenotypes, overview
construction of enzyme-deficient mutant rh57-1, the mutant is affected in the glucose metabolism and shows reduced function of protein synthesis, rh57-1 mutants show resistance to antibiotics, phenotypes, overview
generation of two recombinant variants of DENV NS3: the first single polypeptide mimics the NS2B-NS3 complex containing the full-length NS3 (618 amino acids) linked to the NS2B hydrophilic region (47 amino acids), this variant named NS3-FL, also carried a mutation in the protease catalytic site (H51A) to avoid autoproteolysis. The second variant NS3-hel represents a truncated NS3, containing the helicase domain (amino acids 171 to 618), ATPase/helicase defective NS3-hel mutant (NS3Amut) conserves the RNA annealing activity
generation of two recombinant variants of DENV NS3: the first single polypeptide mimics the NS2B-NS3 complex containing the full-length NS3 (618 amino acids) linked to the NS2B hydrophilic region (47 amino acids), this variant named NS3-FL, also carried a mutation in the protease catalytic site (H51A) to avoid autoproteolysis. The second variant NS3-hel represents a truncated NS3, containing the helicase domain (amino acids 171 to 618), ATPase/helicase defective NS3-hel mutant (NS3Amut) conserves the RNA annealing activity
generation of two recombinant variants of DENV NS3: the first single polypeptide mimics the NS2B-NS3 complex containing the full-length NS3 (618 amino acids) linked to the NS2B hydrophilic region (47 amino acids), this variant named NS3-FL, also carried a mutation in the protease catalytic site (H51A) to avoid autoproteolysis. The second variant NS3-hel represents a truncated NS3, containing the helicase domain (amino acids 171 to 618), ATPase/helicase defective NS3-hel mutant (NS3Amut) conserves the RNA annealing activity
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Rosetta pLac by nickel affinity chromatography, dialysis, and ultrafiltration
gene AtRH57, quantitative RT-PCR enzyme expression analysis, overexpression of His-tagged enzyme in Escherichia coli, transient recombinant expression of EGFP-tagged enzyme in onion cells in the nucleus and nucleolus
AtRH57, a DEAD-box RNA helicase, is involved in feedback inhibition of glucose-mediated abscisic acid accumulation during seedling development and additively affects pre-ribosomal RNA processing with high glucose