3.6.4.B7: RadA recombinase
This is an abbreviated version!
For detailed information about RadA recombinase, go to the full flat file.
Word Map on EC 3.6.4.B7
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3.6.4.B7
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strand
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brca2
-
single-stranded
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meiotic
-
fork
-
checkpoint
-
reca
-
ssdna
-
nucleoprotein
-
helicase
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stall
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radiosensitivity
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non-homologous
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dna-damaging
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fanconi
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radiation-induced
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chromatid
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mre11
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h2ax
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interstrand
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end-joining
-
recombinases
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chk1
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meiosis-specific
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homology-directed
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olaparib
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dna-pkcs
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fancd2
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restart
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prophase
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synaptonemal
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parpis
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error-free
-
reca-like
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unrepaired
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gamma-h2ax
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dsb-induced
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d-loops
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ctip
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break-induced
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translesion
-
holliday
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bard1
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molecular biology
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synthesis
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atr-dependent
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topbp1
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ssdna-binding
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brca1-mutant
-
rucaparib
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diagnostics
-
analysis
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pharmacology
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xrcc4
-
brca1-deficient
- 3.6.4.B7
- strand
- brca2
-
single-stranded
-
meiotic
- fork
-
checkpoint
- reca
- ssdna
- nucleoprotein
- helicase
-
stall
-
radiosensitivity
-
non-homologous
-
dna-damaging
-
fanconi
-
radiation-induced
-
chromatid
- mre11
- h2ax
-
interstrand
-
end-joining
-
recombinases
- chk1
-
meiosis-specific
-
homology-directed
- olaparib
- dna-pkcs
-
fancd2
-
restart
-
prophase
-
synaptonemal
-
parpis
-
error-free
-
reca-like
-
unrepaired
-
gamma-h2ax
-
dsb-induced
-
d-loops
- ctip
-
break-induced
-
translesion
-
holliday
- bard1
- molecular biology
- synthesis
-
atr-dependent
-
topbp1
-
ssdna-binding
-
brca1-mutant
- rucaparib
- diagnostics
- analysis
- pharmacology
- xrcc4
-
brca1-deficient
Reaction
Synonyms
DNA repair and recombination protein, DNA repair protein RAD51 homolog 1, Hvo RadA, MvRadA, Pho RadA, PhoRadA, Rad51, RadA, RadA intein, RadA recombinase, RadA/Sms, RadC1, RadC2, SMS, SSO0250, SsoRadA, SsoRadA recombinase, SsRada
ECTree
3.6.4.B7 RadA recombinaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.6.4.B7 - RadA recombinase
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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
ATP + H2O
ADP + phosphate
at optimal assay conditions, the RadADa presynaptic complex is able to hydrolyze ATP efficiently with ssDNA cofactors of 940 nt and greater. Circular and linearized M13 ssDNA demonstrate the same ability to stimulate ATP hydrolysis as a linearized dsDNA of this phage, whereas the supercoiled dsDNA (replicative form I) is a weak cofactor due to the only partial denaturation at 90°C
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-
?
ATP + H2O
ADP + phosphate
the highly purified enzyme exusively catalyzes single-stranded DNA-dependent ATP hydrolysis, which monitors presynaptic recombinational complex formation, at temperatures above 65°C. The RadA protein alone efficiently promotes the strand exchange reaction at the range of temperatures from 80 to 90°C, i.e., at temperatures approaching the melting point of DNA
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-
?
ATP + H2O
ADP + phosphate
ssDNA-dependent ATPase activity
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-
?
ATP + H2O
ADP + phosphate
both ATP hydrolysis and DNA strand exchange requires accessibility to an active conformation similar to the crystallized ATPase-active form in the presence of ATP, Mg2+ and K+
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-
?
ATP + H2O
ADP + phosphate
single-stranded DNA-dependent ATPase
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-
?
ATP + H2O
ADP + phosphate
the enzyme binds ssDNA, hydrolyzes ATP in a DNA-dependent manner and to catalyzes DNA strand exchange.It shows the ability to bind ssDNA and catalyze DNA strand exchange between ssDNA and homologous linear dsDNA. The ssDNA-dependent ATPase activity displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature
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-
?
ATP + H2O
ADP + phosphate
the enzyme binds ssDNA, hydrolyzes ATP in a DNA-dependent manner and to catalyzes DNA strand exchange.It shows the ability to bind ssDNA and catalyze DNA strand exchange between ssDNA and homologous linear dsDNA. The ssDNA-dependent ATPase activity displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature
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-
?
ATP + H2O
ADP + phosphate
DNA-dependent ATPase, D-loop formation, and strand exchange activities. The enzyme is involved in homologous recombination
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-
?
ATP + H2O
ADP + phosphate
DNA-dependent ATPase, D-loop formation, and strand exchange activities
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-
?
ATP + H2O
ADP + phosphate
the central core domain of RadA is essential for the strand exchange activity and that the N-terminal domain contributes to the enhancement of the reaction efficiency
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-
?
ATP + H2O
ADP + phosphate
the RadA protein is a DNA-dependent ATPase, forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange
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-
?
ATP + H2O
ADP + phosphate
ssDNA-dependent ATPase activity
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-
?
ATP + H2O
ADP + phosphate
the ATPase activity of SsoRadA is ssDNA-dependent. It is suggested that the recombinase first binds ATP, then binds DNA. ATP hydrolysis has no effect on ssDNA binding. After the protein is bound to ssDNA, it hydrolyzes ATP
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-
?
ATP + H2O
ADP + phosphate
the DNA exchange protein RadA displays preference for binding to DNA sequences that are rich in G residues, and under-represented in A and C residues
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-
?
ATP + H2O
ADP + phosphate
the RadA protein is a ssDNA-dependent ATPase. ATP hydrolysis is less efficient in the presence of double-stranded DNA, and almost no hydrolysis occurs in the absence of DNA. It forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange
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-
?
ATP + H2O
ADP + phosphate
SsoRadA ssDNA-dependent ATPase activity
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-
?
ATP + H2O
ADP + phosphate
the ATPase activity of SsoRadA is ssDNA-dependent. It is suggested that the recombinase first binds ATP, then binds DNA. ATP hydrolysis has no effect on ssDNA binding. After the protein is bound to ssDNA, it hydrolyzes ATP
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-
?
ATP + H2O
ADP + phosphate
the RadA protein is a DNA-dependent ATPase, forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange
-
-
?
ATP + H2O
ADP + phosphate
the RadA protein is a ssDNA-dependent ATPase. ATP hydrolysis is less efficient in the presence of double-stranded DNA, and almost no hydrolysis occurs in the absence of DNA. It forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange
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-
?
ATP + H2O
ADP + phosphate
the DNA exchange protein RadA displays preference for binding to DNA sequences that are rich in G residues, and under-represented in A and C residues
-
-
?
ATP + H2O
ADP + phosphate
SsoRadA ssDNA-dependent ATPase activity
-
-
?
ATP + H2O
AMP + diphosphate
the enzyme catalyses efficient D-loop formation and strand exchange at temperatures of 60-70°C, capable of promoting strand transfer through at least 1200 bp of duplex DNA
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-
?
ATP + H2O
AMP + diphosphate
ATPase activity is most efficient in presence of ssDNA, it is considerably reduced in presence of dsDNA and virtually no ATP is hydrolysed in absence of DNA. The enzyme catalyses efficient D-loop formation and strand exchange at temperatures of 60-70°C, capable of promoting strand transfer through at least 1200 bp of duplex DNA
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?
additional information
?
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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?
additional information
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performance of transformation and survival assays, DNA helicase assays, ATP hydrolysis assays, and protein-DNA or protein-protein interactions analysis
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additional information
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performance of transformation and survival assays, DNA helicase assays, ATP hydrolysis assays, and protein-DNA or protein-protein interactions analysis
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additional information
?
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performance of transformation and survival assays, DNA helicase assays, ATP hydrolysis assays, and protein-DNA or protein-protein interactions analysis
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additional information
?
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an NADH-coupled assay is used to measure the ATPase activity of RadA, in the presence or absence of various DNA cofactors, circular ssDNA (jX174 virion) and dsDNA (jX174 RF DNA). DNA substrate specificity of RadA binding, overview. The wild-type RadA protein preferentially binds single-strand DNA in the presence of ADP. Binding preference for by poly(dT) by RadA and also by RecA. RadA is observed to bind poly(dT)30 when flanked on both 5' and 3' ends by 30 nucleotides of natural DNA sequence. Catalysis of RecA-mediated strand-exchange reactions between 5386 nucleotide circular jX174 ssDNA and linear duplex DNA in the presence of ATP and an ATP-regeneration system, ATP hydrolysis in reactions including RecA, SSB and RadA
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additional information
?
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an NADH-coupled assay is used to measure the ATPase activity of RadA, in the presence or absence of various DNA cofactors, circular ssDNA (jX174 virion) and dsDNA (jX174 RF DNA). DNA substrate specificity of RadA binding, overview. The wild-type RadA protein preferentially binds single-strand DNA in the presence of ADP. Binding preference for by poly(dT) by RadA and also by RecA. RadA is observed to bind poly(dT)30 when flanked on both 5' and 3' ends by 30 nucleotides of natural DNA sequence. Catalysis of RecA-mediated strand-exchange reactions between 5386 nucleotide circular jX174 ssDNA and linear duplex DNA in the presence of ATP and an ATP-regeneration system, ATP hydrolysis in reactions including RecA, SSB and RadA
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additional information
?
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monomeric RAD51 is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. AMPPNP binds to RAD51, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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-
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additional information
?
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
-
-
?
additional information
?
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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-
?
additional information
?
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monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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-
-
additional information
?
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to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
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-
additional information
?
-
to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
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additional information
?
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monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
-
-
-
additional information
?
-
to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
-
-
-
additional information
?
-
monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
-
-
-
additional information
?
-
to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
-
-
-
additional information
?
-
monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
-
-
-
additional information
?
-
to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
-
-
-
additional information
?
-
monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
-
-
-
additional information
?
-
to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
-
-
-
additional information
?
-
monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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additional information
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enzyme RadA binds both to ssDNA and dsDNA. The highly thermostable RadA protein from the archaeon Pyrococcus woesei enhances the specificity of simplex and multiplex PCR assays
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additional information
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enzyme RadA binds both to ssDNA and dsDNA. The highly thermostable RadA protein from the archaeon Pyrococcus woesei enhances the specificity of simplex and multiplex PCR assays
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additional information
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formation of SsoRadA-ssDNA complexes resulting in SsoRadA nucleoprotein filaments
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additional information
?
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formation of SsoRadA-ssDNA complexes resulting in SsoRadA nucleoprotein filaments
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?
additional information
?
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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formation of SsoRadA-ssDNA complexes
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additional information
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formation of SsoRadA-ssDNA complexes
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
?
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
?
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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-
additional information
?
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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?
additional information
?
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formation of SsoRadA-ssDNA complexes resulting in SsoRadA nucleoprotein filaments
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?
additional information
?
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formation of SsoRadA-ssDNA complexes
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?
additional information
?
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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-
-
additional information
?
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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?
additional information
?
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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-
?
additional information
?
-
The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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