The role of stress proteins in the protein biosynthesis.

应激蛋白在蛋白质生物合成中的作用。

基本信息

批准号：
04044100
负责人：
NAGATA Kazuhiro
金额：
$ 2.88万
依托单位：
Kyoto University
依托单位国家：
日本
项目类别：
Grant-in-Aid for international Scientific Research
财政年份：
1992
资助国家：
日本
起止时间：
1992 至 1993
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-04044100/
关键词：
Stress protein Heat shock transcription factor Molecular Chaperone コラーゲン小胞体

项目摘要

1. Nagata and Morimoto collaborated to investigate the regulatory mechanism of the expression of stress proteins through heat shock transcription factor (HSF). Previously, HSF1 and HSF2 were identified and cloned. We have cloned a cDNA encoding a novel heat shock factor, HSF3, from the cDNA library of chick cells in addition to the chick homologues of human HSF1 and HSF2. HSF3 was activated by heat shock in chick erythrocytic cell line, but not in other chick cells. However, it has been revealed that HSF3 can synergistically cooperate with HSF1 in the activation of stress-induced transcription of stress proteins.2. Nagata and Hirayoshi investigated the interaction of collagen-specific stress protein, HSP47, with newly synthesized procollagens in the cells. The purpose of the study this year was focused to where the procollagen associates with and dissociates from HSP47 during its biosynthesis. It has been revealed that procollagen binds to HSP47 in the endplasmic reticulum (ER) immediately after the procollagen co-translationally enters the ER, and dissociates from HSP47 in the cis-golgi network after the procollagen is transported into the golgi area.3. Welch, Bensaude and Morimoto investigated the interaction of HSP70 with newly synthesized proteins as well as with HSFs. During the period of this project, it was figured out that HSP70 associates with activated DNA-binding HSF and renders the dissociation of HSF from the DNA resulting in the attenuation of the HSF activation after the completion of the induction of stress proteins including HSP70.

1. Nagata和Morimoto合作研究了通过热休克转录因子（HSF）调节应激蛋白表达的机制。此前，HSF1和HSF2已被鉴定和克隆。除了人 HSF1 和 HSF2 的鸡同源物之外，我们还从鸡细胞 cDNA 文库中克隆了编码新型热休克因子 HSF3 的 cDNA。 HSF3 在鸡红细胞系中被热休克激活，但在其他鸡细胞中则不然。然而，研究表明HSF3可以与HSF1协同作用，激活应激诱导的应激蛋白转录。 2． Nagata 和 Hirayoshi 研究了胶原蛋白特异性应激蛋白 HSP47 与细胞中新合成的前胶原蛋白的相互作用。今年研究的目的集中于前胶原蛋白在生物合成过程中与 HSP47 结合和解离的位置。研究表明，原胶原共翻译进入内质网(ER)后立即与HSP47结合，并在原胶原转运至高尔基体区域后与顺式高尔基体网络中的HSP47解离。3． Welch、Bensaude 和 Morimoto 研究了 HSP70 与新合成的蛋白质以及 HSF 的相互作用。在该项目期间，发现HSP70与激活的DNA结合HSF结合，并导致HSF从DNA解离，导致包括HSP70在内的应激蛋白诱导完成后HSF激活减弱。