The life of [PSI].

The life of [PSI].
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[psi]的生活。

DOI:
10.1007/s00294-017-0714-7
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发表时间:
2018-03
期刊:
影响因子:
2.5
通讯作者:
Tuite M
Tuite M
中科院分区:
生物学3区
文献类型:
--
作者:
Cox B;Tuite M

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酿酒酵母AAA+解聚酶Hsp104对几乎所有已知的酿酒酵母蛋白的维持和遗传都是必不可少的。对于Sup35蛋白的Prion形式[Psi+]来说,独特的是,Hsp104似乎有两种活动,涉及不同的辅助伴侣,通过这两种活动影响Sup35蛋白的Prion形式[Psi+]的遗传。每条途径也参与了对衰老的保护,一条途径是通过分解受损的蛋白质,另一条途径是通过在萌芽期间将蛋白质保留在母细胞中。Hsp104和Sup35的突变都通过这些途径中的一条或另一条影响Pron的遗传,在营养(萌芽)分裂和孢子形成过程中,Hsp104酶活性或表达的操纵也是如此。根据我们最近的发现(Ness等人)在Molec Microbiol 104:125-143中,我们认为,在孢子形成过程中[PSI+]细胞中可遗传的Prion形式Sup35的管理可能是Hsp104在孢子形成过程中恢复活力的一个标志。
The AAA+ disaggregase Hsp104 is essential for the maintenance and inheritance of nearly all known prions of the yeast Saccharomyces cerevisiae. Uniquely for [PSI +], the prion form of the Sup35 protein, there seem to be two activities, involving differing co-chaperones, by which Hsp104 affects the inheritance of [PSI +], the prion form of the Sup35 protein. Each pathway is also involved in protection against ageing, one through disaggregation of damaged proteins and the other through their retention in the mother cell during budding. Mutations in both Hsp104 and Sup35 affect prion inheritance by one or other of these pathways, as does manipulation of either Hsp104 enzyme activity or expression, in both vegetative (budding) divisions and in sporulation. Based on our recent finding (Ness et al. in Molec Microbiol 104:125–143,) we suggest that the management of the heritable prion forms of Sup35 in [PSI +] cells in sporulation may be a marker for a role for Hsp104 in rejuvenation during sporulation.
DOI: 10.1038/214764a0
发表时间: 1967-01-01
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