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A virus capsid‐like nanocompartment that stores iron and protects bacteria from oxidative stress

机译:一种病毒衣壳样纳米组合,物料储存熨斗和保护细菌免受氧化应激

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摘要

Living cells compartmentalize materials and enzymatic reactions to increase metabolic efficiency. While eukaryotes use membrane-bound organelles, bacteria and archaea rely primarily on protein-bound nanocompartments. Encapsulins constitute a class of nanocompartments widespread in bacteria and archaea whose functions have hitherto been unclear. Here, we characterize the encapsulin nanocompartment from Myxococcus xanthus, which consists of a shell protein (EncA, 32.5 kDa) and three internal proteins (EncB, 17 kDa; EncC, 13 kDa; EncD, 11 kDa). Using cryo-electron microscopy, we determined that EncA self-assembles into an icosahedral shell 32 nm in diameter (26 nm internal diameter), built from 180 subunits with the fold first observed in bacteriophage HK97 capsid. The internal proteins, of which EncB and EncC have ferritin-like domains, attach to its inner surface. Native nanocompartments have dense iron-rich cores. Functionally, they resemble ferritins, cage-like iron storage proteins, but with a massively greater capacity (∼30,000 iron atoms versus ∼3,000 in ferritin). Physiological data reveal that few nanocompartments are assembled during vegetative growth, but they increase fivefold upon starvation, protecting cells from oxidative stress through iron sequestration. Synopsis Bacteria compartmentalize by sequestering components into protein shells. Here, such a nanocompartment is shown to structurally resemble virus capsids and to store large amounts of iron for protection under starvation conditions. Iron homeostasis in Myxococcus xanthus involves iron sequestration into large protein shells (encapsulin nanocompartments). The shell is lined with adaptor proteins with ferritin-like folds that nucleate iron-rich granules. The encapsulin system appears to complement a ferritin system. The encapsulin shell closely resembles capsids of bacteriophages and herpesvirus. Thus, phages may have arisen from cellular genes, or M. xanthus may have acquired the encapsulin shell gene from a bacteriophage. Bacteria compartmentalize by sequestering components into protein shells. Here, such a nanocompartment is shown to structurally resemble virus capsids and to store large amounts of iron for protection under starvation conditions.
机译:活细胞分区材料和酶促反应以提高代谢效率。虽然真核生物使用膜结合的细胞器,细菌和古代依赖于蛋白质结合的纳米组分。密封蛋白素构成一类纳米组分在细菌和古群中普遍存在的,其功能迄今为止尚不清楚。在这里,我们将密封蛋白酶纳米组织从麦蛋白酶蛋白(Enca,32.5kDa)和三个内部蛋白质(Encb,17kDa; encc,13kDa; Encd,11 kda)组成。使用冷冻电子显微镜,我们确定Enca自组装成直径(26nm内径)的IcosaheDral壳32nm,从180个亚基建造,折叠在噬菌体HK97衣壳中首先观察到。内部蛋白质,其ENCB和ENCC具有含铁蛋白样域,附着于其内表面。本土纳米组分具有密集的铁核心。在功能上,它们类似于铁蛋白,笼状的铁储存蛋白,但具有大量的容量(〜30,000铁原子与〜3,000在铁蛋白中)。生理数据显示,在营养生长期间组装了很少的纳米组合,但它们在饥饿后增加五倍,通过铁螯合保护细胞免受氧化胁迫。通过螯合成分在蛋白质壳中的综述细胞分区。这里,这种纳米可分量显示在结构上类似于病毒衣壳,并在饥饿条件下存储大量铁用于保护。 Myxococcus Xanthus的铁稳态涉及将铁螯合成大型蛋白质壳(包封蛋白纳米组分)。壳体衬有含有铁蛋白蛋白的适配器蛋白,含有富含铁的颗粒颗粒。包封系统似乎补充了铁蛋白系统。包封蛋白壳非常类似于噬菌体和疱疹病毒的衣壳。因此,噬菌体可能从细胞基因中出现,或者Xanthus可以从噬菌体中获得密封蛋白酶壳基因。通过螯合成分在蛋白质壳中分隔细胞。这里,这种纳米可分量显示在结构上类似于病毒衣壳,并在饥饿条件下存储大量铁用于保护。

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