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Tomitake Tsukihara - One of the best experts on this subject based on the ideXlab platform.
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a vault Ribonucleoprotein Particle exhibiting 39 fold dihedral symmetry corrigendum
Acta Crystallographica Section D-biological Crystallography, 2009Co-Authors: Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, M Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake TsukiharaAbstract:In the article by Kato et al. (2008 ▶), the values for ϕ and ψ were transposed. Throughout the paper (ϕ, ψ) = (90°, 110°) should be replaced by (ϕ, ψ) = (110°, 90°). Also, in Fig. 4 of the article the label ϕ in parts (a) and (b) should be replaced by ψ. In addition, on page 530 of the article the size of the vault Particles was given as 400 × 40 × 700 A when it should be 400 × 400 × 700 A.
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a vault Ribonucleoprotein Particle exhibiting 39 fold dihedral symmetry
Acta Crystallographica Section D-biological Crystallography, 2008Co-Authors: Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, M Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake TsukiharaAbstract:Vault is a 12.9 MDa Ribonucleoprotein Particle with a barrel-like shape, two protruding caps and an invaginated waist structure that is highly conserved in a wide variety of eukaryotes. Multimerization of the major vault protein (MVP) is sufficient to assemble the entire exterior shell of the barrel-shaped vault Particle. Multiple copies of two additional proteins, vault poly(ADP-ribose) polymerase (VPARP) and telomerase-associated protein 1 (TEP1), as well as a small vault RNA (vRNA), are also associated with vault. Here, the crystallization of vault Particles is reported. The crystals belong to space group C2, with unit-cell parameters a = 708.0, b = 385.0, c = 602.9 A, β = 124.8°. Rotational symmetry searches based on the R factor and correlation coefficient from noncrystallographic symmetry (NCS) averaging indicated that the Particle has 39-fold dihedral symmetry.
Koji Kato - One of the best experts on this subject based on the ideXlab platform.
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a vault Ribonucleoprotein Particle exhibiting 39 fold dihedral symmetry corrigendum
Acta Crystallographica Section D-biological Crystallography, 2009Co-Authors: Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, M Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake TsukiharaAbstract:In the article by Kato et al. (2008 ▶), the values for ϕ and ψ were transposed. Throughout the paper (ϕ, ψ) = (90°, 110°) should be replaced by (ϕ, ψ) = (110°, 90°). Also, in Fig. 4 of the article the label ϕ in parts (a) and (b) should be replaced by ψ. In addition, on page 530 of the article the size of the vault Particles was given as 400 × 40 × 700 A when it should be 400 × 400 × 700 A.
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a vault Ribonucleoprotein Particle exhibiting 39 fold dihedral symmetry
Acta Crystallographica Section D-biological Crystallography, 2008Co-Authors: Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, M Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake TsukiharaAbstract:Vault is a 12.9 MDa Ribonucleoprotein Particle with a barrel-like shape, two protruding caps and an invaginated waist structure that is highly conserved in a wide variety of eukaryotes. Multimerization of the major vault protein (MVP) is sufficient to assemble the entire exterior shell of the barrel-shaped vault Particle. Multiple copies of two additional proteins, vault poly(ADP-ribose) polymerase (VPARP) and telomerase-associated protein 1 (TEP1), as well as a small vault RNA (vRNA), are also associated with vault. Here, the crystallization of vault Particles is reported. The crystals belong to space group C2, with unit-cell parameters a = 708.0, b = 385.0, c = 602.9 A, β = 124.8°. Rotational symmetry searches based on the R factor and correlation coefficient from noncrystallographic symmetry (NCS) averaging indicated that the Particle has 39-fold dihedral symmetry.
John Abelson - One of the best experts on this subject based on the ideXlab platform.
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purification of the yeast u4 u6 u5 small nuclear Ribonucleoprotein Particle and identification of its proteins
Proceedings of the National Academy of Sciences of the United States of America, 1999Co-Authors: Scott W. Stevens, John AbelsonAbstract:The yeast U4/U6⋅U5 pre-mRNA splicing small nuclear Ribonucleoprotein (snRNP) is a 25S small nuclear Ribonucleoprotein Particle similar in size, composition, and morphology to its counterpart in human cells. The yeast U4/U6⋅U5 snRNP complex has been purified to near homogeneity by affinity chromatography and preparative glycerol gradient sedimentation. We show that there are at least 24 proteins stably associated with this Particle and performed mass spectrometry microsequencing to determine their identities. In addition to the seven canonical core Sm proteins, there are a set of U6 snRNP specific Sm proteins, eight previously described U4/U6⋅U5 snRNP proteins, and four novel proteins. Two of the novel proteins have likely RNA binding properties, one has been implicated in the cell cycle, and one has no identifiable sequence homologues or functional motifs. The purification of the low abundance U4/U6⋅U5 snRNP from yeast and the powerful sequencing methodologies using small amounts of protein make possible the rapid identification of novel and previously unidentified components of large, low-abundance macromolecular machines from any genetically manipulable organism.
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a u5 small nuclear Ribonucleoprotein Particle protein involved only in the second step of pre mrna splicing in saccharomyces cerevisiae
Molecular and Cellular Biology, 1993Co-Authors: David S Horowitz, John AbelsonAbstract:The PRP18 gene, which had been identified in a screen for pre-mRNA splicing mutants in Saccharomyces cerevisiae, has been cloned and sequenced. Yeast strains bearing only a disrupted copy of PRP18 are temperature sensitive for growth; even at a low temperature, they grow extremely slowly and do not splice pre-mRNA efficiently. This unusual temperature sensitivity can be reproduced in vitro; extracts immunodepleted of PRP18 are temperature sensitive for the second step of splicing. The PRP18 protein has been overexpressed in active form in Escherichia coli and has been purified to near homogeneity. Antibodies directed against PRP18 precipitate the U4/U5/U6 small nuclear Ribonucleoprotein Particle (snRNP) from yeast extracts. From extracts depleted of the U6 small nuclear RNA (snRNA), the U4 and U5 snRNAs can be immunoprecipitated, while no snRNAs can be precipitated from extracts depleted of the U5 snRNA. PRP18 therefore appears to be primarily associated with the U5 snRNP. The antibodies against PRP18 inhibit the second step of pre-mRNA splicing in vitro. Together, these results imply that the U5 snRNP plays a role in the second step of splicing and suggest a model for the action of PRP18.
Hideaki Tanaka - One of the best experts on this subject based on the ideXlab platform.
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a vault Ribonucleoprotein Particle exhibiting 39 fold dihedral symmetry corrigendum
Acta Crystallographica Section D-biological Crystallography, 2009Co-Authors: Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, M Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake TsukiharaAbstract:In the article by Kato et al. (2008 ▶), the values for ϕ and ψ were transposed. Throughout the paper (ϕ, ψ) = (90°, 110°) should be replaced by (ϕ, ψ) = (110°, 90°). Also, in Fig. 4 of the article the label ϕ in parts (a) and (b) should be replaced by ψ. In addition, on page 530 of the article the size of the vault Particles was given as 400 × 40 × 700 A when it should be 400 × 400 × 700 A.
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a vault Ribonucleoprotein Particle exhibiting 39 fold dihedral symmetry
Acta Crystallographica Section D-biological Crystallography, 2008Co-Authors: Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, M Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake TsukiharaAbstract:Vault is a 12.9 MDa Ribonucleoprotein Particle with a barrel-like shape, two protruding caps and an invaginated waist structure that is highly conserved in a wide variety of eukaryotes. Multimerization of the major vault protein (MVP) is sufficient to assemble the entire exterior shell of the barrel-shaped vault Particle. Multiple copies of two additional proteins, vault poly(ADP-ribose) polymerase (VPARP) and telomerase-associated protein 1 (TEP1), as well as a small vault RNA (vRNA), are also associated with vault. Here, the crystallization of vault Particles is reported. The crystals belong to space group C2, with unit-cell parameters a = 708.0, b = 385.0, c = 602.9 A, β = 124.8°. Rotational symmetry searches based on the R factor and correlation coefficient from noncrystallographic symmetry (NCS) averaging indicated that the Particle has 39-fold dihedral symmetry.
Tomoyuki Sumizawa - One of the best experts on this subject based on the ideXlab platform.
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a vault Ribonucleoprotein Particle exhibiting 39 fold dihedral symmetry corrigendum
Acta Crystallographica Section D-biological Crystallography, 2009Co-Authors: Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, M Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake TsukiharaAbstract:In the article by Kato et al. (2008 ▶), the values for ϕ and ψ were transposed. Throughout the paper (ϕ, ψ) = (90°, 110°) should be replaced by (ϕ, ψ) = (110°, 90°). Also, in Fig. 4 of the article the label ϕ in parts (a) and (b) should be replaced by ψ. In addition, on page 530 of the article the size of the vault Particles was given as 400 × 40 × 700 A when it should be 400 × 400 × 700 A.
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a vault Ribonucleoprotein Particle exhibiting 39 fold dihedral symmetry
Acta Crystallographica Section D-biological Crystallography, 2008Co-Authors: Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, M Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake TsukiharaAbstract:Vault is a 12.9 MDa Ribonucleoprotein Particle with a barrel-like shape, two protruding caps and an invaginated waist structure that is highly conserved in a wide variety of eukaryotes. Multimerization of the major vault protein (MVP) is sufficient to assemble the entire exterior shell of the barrel-shaped vault Particle. Multiple copies of two additional proteins, vault poly(ADP-ribose) polymerase (VPARP) and telomerase-associated protein 1 (TEP1), as well as a small vault RNA (vRNA), are also associated with vault. Here, the crystallization of vault Particles is reported. The crystals belong to space group C2, with unit-cell parameters a = 708.0, b = 385.0, c = 602.9 A, β = 124.8°. Rotational symmetry searches based on the R factor and correlation coefficient from noncrystallographic symmetry (NCS) averaging indicated that the Particle has 39-fold dihedral symmetry.
