Structural studies of large nucleoprotein particles, vaults.

Structural studies of large nucleoprotein particles, vaults.
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DOI:
10.2183/pjab.88.416
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发表时间:
2012
期刊:
Proceedings of the Japan Academy. Series B, Physical and biological sciences
影响因子:
--
通讯作者:
Tsukihara T
Tsukihara T
中科院分区:
其他
文献类型:
--
作者:
Tanaka H;Tsukihara T

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Vault 是迄今为止描述的最大的非二十面体胞质核蛋白颗粒。穹窿的广泛存在和进化保护表明了重要的生物学作用,尽管它们的功能尚未完全阐明。大鼠肝脏穹窿的 X 射线结构以 3.5 Å 分辨率测定。它呈卵圆形,尺寸为 40 × 40 × 67 nm3。穹窿的笼状结构由半穹窿二聚体组成,每个半穹窿包含39条相同的主要穹窿蛋白(MVP)链。每个 MVP 单体折叠成 12 个结构域:9 个结构重复结构域、一个肩结构域、一个帽螺旋结构域和一个帽环结构域。 42 圈长的帽螺旋结构域之间的相互作用是稳定颗粒的关键。通过电子显微镜观察,穹窿的其他成分、端粒酶相关蛋白、聚(ADP-核糖)聚合酶和小RNA位于穹窿颗粒中。
Vault is the largest nonicosahedral cytosolic nucleoprotein particle ever described. The widespread presence and evolutionary conservation of vaults suggest important biologic roles, although their functions have not been fully elucidated. X-ray structure of vault from rat liver was determined at 3.5 Å resolution. It exhibits an ovoid shape with a size of 40 × 40 × 67 nm3. The cage structure of vault consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains. Each MVP monomer folds into 12 domains: nine structural repeat domains, a shoulder domain, a cap-helix domain and a cap-ring domain. Interactions between the 42-turn-long cap-helix domains are key to stabilizing the particle. The other components of vaults, telomerase-associated proteins, poly(ADP-ribose) polymerases and small RNAs, are in location in the vault particle by electron microscopy.
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