The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Kosuke Morikawa - One of the best experts on this subject based on the ideXlab platform.
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a unique β hairpin protruding from aaa atpase domain of ruvb Motor Protein is involved in the interaction with ruva dna recognition Protein for branch migration of holliday junctions
Journal of Biological Chemistry, 2001Co-Authors: Yongwoon Han, Hiroshi Iwasaki, Kosuke Morikawa, Kazuhiro Yamada, Kouta Mayanagi, Tomoko Miyata, Hideo ShinagawaAbstract:Abstract The Escherichia coli RuvB Protein is a Motor Protein that forms a complex with RuvA and promotes branch migration of Holliday junctions during homologous recombination. This study describes the characteristics of two RuvB mutants, I148T and I150T, that do not promote branch migration in the presence of RuvA. These RuvB mutants hydrolyzed ATP and bound duplex DNA with the same efficiency as wild-type RuvB, but the mutants did not form a complex with RuvA and were defective in loading onto junction DNA in a RuvA-assisted manner. A recent crystallographic study revealed that Ile148 and Ile150 are in a unique β-hairpin that protrudes from the AAA+ ATPase domain of RuvB. We propose that this β-hairpin interacts with hydrophobic residues in the mobile third domain of RuvA and that this interaction is vital for the RuvA-assisted loading of RuvB onto Holliday junction DNA.
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crystal structure of the holliday junction migration Motor Protein ruvb from thermus thermophilus hb8
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Kazuhiro Yamada, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, N Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Kosuke MorikawaAbstract:We report here the crystal structure of the RuvB Motor Protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition Protein RuvA may bind a flexible β-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of Motor Protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
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crystal structure of the holliday junction migration Motor Protein ruvb from thermus thermophilus hb8
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Kazuhiro Yamada, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, N Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Kosuke MorikawaAbstract:We report here the crystal structure of the RuvB Motor Protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition Protein RuvA may bind a flexible beta-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of Motor Protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
Kazuhiro Yamada - One of the best experts on this subject based on the ideXlab platform.
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a unique β hairpin protruding from aaa atpase domain of ruvb Motor Protein is involved in the interaction with ruva dna recognition Protein for branch migration of holliday junctions
Journal of Biological Chemistry, 2001Co-Authors: Yongwoon Han, Hiroshi Iwasaki, Kosuke Morikawa, Kazuhiro Yamada, Kouta Mayanagi, Tomoko Miyata, Hideo ShinagawaAbstract:Abstract The Escherichia coli RuvB Protein is a Motor Protein that forms a complex with RuvA and promotes branch migration of Holliday junctions during homologous recombination. This study describes the characteristics of two RuvB mutants, I148T and I150T, that do not promote branch migration in the presence of RuvA. These RuvB mutants hydrolyzed ATP and bound duplex DNA with the same efficiency as wild-type RuvB, but the mutants did not form a complex with RuvA and were defective in loading onto junction DNA in a RuvA-assisted manner. A recent crystallographic study revealed that Ile148 and Ile150 are in a unique β-hairpin that protrudes from the AAA+ ATPase domain of RuvB. We propose that this β-hairpin interacts with hydrophobic residues in the mobile third domain of RuvA and that this interaction is vital for the RuvA-assisted loading of RuvB onto Holliday junction DNA.
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crystal structure of the holliday junction migration Motor Protein ruvb from thermus thermophilus hb8
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Kazuhiro Yamada, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, N Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Kosuke MorikawaAbstract:We report here the crystal structure of the RuvB Motor Protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition Protein RuvA may bind a flexible β-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of Motor Protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
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crystal structure of the holliday junction migration Motor Protein ruvb from thermus thermophilus hb8
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Kazuhiro Yamada, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, N Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Kosuke MorikawaAbstract:We report here the crystal structure of the RuvB Motor Protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition Protein RuvA may bind a flexible beta-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of Motor Protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
Hideo Shinagawa - One of the best experts on this subject based on the ideXlab platform.
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a unique β hairpin protruding from aaa atpase domain of ruvb Motor Protein is involved in the interaction with ruva dna recognition Protein for branch migration of holliday junctions
Journal of Biological Chemistry, 2001Co-Authors: Yongwoon Han, Hiroshi Iwasaki, Kosuke Morikawa, Kazuhiro Yamada, Kouta Mayanagi, Tomoko Miyata, Hideo ShinagawaAbstract:Abstract The Escherichia coli RuvB Protein is a Motor Protein that forms a complex with RuvA and promotes branch migration of Holliday junctions during homologous recombination. This study describes the characteristics of two RuvB mutants, I148T and I150T, that do not promote branch migration in the presence of RuvA. These RuvB mutants hydrolyzed ATP and bound duplex DNA with the same efficiency as wild-type RuvB, but the mutants did not form a complex with RuvA and were defective in loading onto junction DNA in a RuvA-assisted manner. A recent crystallographic study revealed that Ile148 and Ile150 are in a unique β-hairpin that protrudes from the AAA+ ATPase domain of RuvB. We propose that this β-hairpin interacts with hydrophobic residues in the mobile third domain of RuvA and that this interaction is vital for the RuvA-assisted loading of RuvB onto Holliday junction DNA.
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crystal structure of the holliday junction migration Motor Protein ruvb from thermus thermophilus hb8
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Kazuhiro Yamada, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, N Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Kosuke MorikawaAbstract:We report here the crystal structure of the RuvB Motor Protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition Protein RuvA may bind a flexible β-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of Motor Protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
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crystal structure of the holliday junction migration Motor Protein ruvb from thermus thermophilus hb8
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Kazuhiro Yamada, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, N Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Kosuke MorikawaAbstract:We report here the crystal structure of the RuvB Motor Protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition Protein RuvA may bind a flexible beta-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of Motor Protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
Varuni Subramaniam - One of the best experts on this subject based on the ideXlab platform.
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translocation of double stranded dna through membrane adapted phi29 Motor Protein nanopores
Nature Nanotechnology, 2009Co-Authors: David Wendell, Varuni Subramaniam, Peng Jing, Jia Geng, Carlo D. MontemagnoAbstract:Proteins isolated from a specific type of virus have channels that are wide enough to allow double-stranded DNA to pass through, offering a new conductive biological pore for various applications including DNA sequencing.
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translocation of double stranded dna through membrane adapted phi29 Motor Protein nanopores
Nature Nanotechnology, 2009Co-Authors: David Wendell, Varuni Subramaniam, Peng Jing, Carlo D. Montemagno, Jia Geng, Tae Jin Lee, Peixuan GuoAbstract:Biological pores have been used to study the transport of DNA and other molecules, but most pores have channels that allow only the movement of small molecules and single-stranded DNA and RNA. The bacteriophage phi29 DNA-packaging Motor, which allows double-stranded DNA to enter the virus during maturation and exit during an infection, contains a connector Protein with a channel that is between 3.6 and 6 nm wide. Here we show that a modified version of this connector Protein, when reconstituted into liposomes and inserted into planar lipid bilayers, allows the translocation of double-stranded DNA. The measured conductance of a single connector channel was 4.8 nS in 1 M KCl. This engineered and membrane-adapted phage connector is expected to have applications in microelectromechanical sensing, microreactors, gene delivery, drug loading and DNA sequencing.
Hiroshi Iwasaki - One of the best experts on this subject based on the ideXlab platform.
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a unique β hairpin protruding from aaa atpase domain of ruvb Motor Protein is involved in the interaction with ruva dna recognition Protein for branch migration of holliday junctions
Journal of Biological Chemistry, 2001Co-Authors: Yongwoon Han, Hiroshi Iwasaki, Kosuke Morikawa, Kazuhiro Yamada, Kouta Mayanagi, Tomoko Miyata, Hideo ShinagawaAbstract:Abstract The Escherichia coli RuvB Protein is a Motor Protein that forms a complex with RuvA and promotes branch migration of Holliday junctions during homologous recombination. This study describes the characteristics of two RuvB mutants, I148T and I150T, that do not promote branch migration in the presence of RuvA. These RuvB mutants hydrolyzed ATP and bound duplex DNA with the same efficiency as wild-type RuvB, but the mutants did not form a complex with RuvA and were defective in loading onto junction DNA in a RuvA-assisted manner. A recent crystallographic study revealed that Ile148 and Ile150 are in a unique β-hairpin that protrudes from the AAA+ ATPase domain of RuvB. We propose that this β-hairpin interacts with hydrophobic residues in the mobile third domain of RuvA and that this interaction is vital for the RuvA-assisted loading of RuvB onto Holliday junction DNA.
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crystal structure of the holliday junction migration Motor Protein ruvb from thermus thermophilus hb8
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Kazuhiro Yamada, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, N Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Kosuke MorikawaAbstract:We report here the crystal structure of the RuvB Motor Protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition Protein RuvA may bind a flexible β-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of Motor Protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
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crystal structure of the holliday junction migration Motor Protein ruvb from thermus thermophilus hb8
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Kazuhiro Yamada, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, N Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Kosuke MorikawaAbstract:We report here the crystal structure of the RuvB Motor Protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition Protein RuvA may bind a flexible beta-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of Motor Protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.