Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae.
Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae.
复制标题
酿酒酵母细胞骨架组装蛋白 sla1 和释放因子 Sup35 (eRF3) 朊病毒形成域之间相互作用的遗传学研究。
DOI：
10.1093/genetics/153.1.81
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发表时间：
1999
期刊：
影响因子：
3.3
通讯作者：
Chernoff,YO
中科院分区：
文献类型：
--
作者：
Bailleul,PA;Newnam,GP;Steenbergen,JN;Chernoff,YO
Striking similarities between cytoskeletal assembly and the “nucleated polymerization” model of prion propagation suggest that similar or overlapping sets of proteins may assist in both processes. We show that the C-terminal domain of the yeast cytoskeletal assembly protein Sla1 (Sla1C) specifically interacts with the N-terminal prion-forming domain (Sup35N) of the yeast release factor Sup35 (eRF3) in the two-hybrid system. Sla1C and several other Sup35N-interacting proteins also exhibit two-hybrid interactions with the poly-Gln-expanded N-proximal fragment of human huntingtin, which promotes Huntington disease-associated aggregation. The Sup35N-Sla1C interaction is inhibited by Sup35N alterations that make Sup35 unable to propagate the [PSI+] state and by the absence of the chaperone protein Hsp104, which is essential for [PSI] propagation. In a Sla1–background, [PSI] curing by dimethylsulfoxide or excess Hsp104 is increased, while translational readthrough and de novo [PSI] formation induced by excess Sup35 or Sup35N are decreased. These data show that, in agreement with the proposed function of Sla1 during cytoskeletal formation, Sla1 assists in [PSI] formation and propagation, but is not required for these processes. Sla1–strains are sensitive to some translational inhibitors, and some sup35 mutants, obtained in a Sla1–background, are sensitive to Sla1, suggesting that the interaction between Sla1 and Sup35 proteins may play a role in the normal function of the translational apparatus. We hypothesize that Sup35N is involved in regulatory interactions with intracellular structural networks, and [PSI] prion may be formed as a by-product of this process.
