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热休克诱导的蛋白水解抑制:聚腺苷酸结合蛋白的降解模式可能会错误地表明其在热休克期间的特异性丢失。

Heat shock-induced repression of proteolysis: poly(A)-binding protein degradation patterns can illusorily suggest its specific loss during heat shock.

作者信息

Lefrère V, Duncan R F

机构信息

Centre de Biologie du Developpement, Bat. IVR3, Universite Paul Sabatier, Toulouse, France.

出版信息

Nucleic Acids Res. 1994 May 11;22(9):1640-2. doi: 10.1093/nar/22.9.1640.

Abstract

Poly(A)-binding protein (PABP) is highly susceptible to proteolysis during cell lysis of Drosophila tissue culture cells unless substantial amounts of proteolysis inhibitors are included in the extraction buffer. This intrinsic proteolytic activity is substantially reduced during heat shock. An artifactual appearance that poly(A)-binding protein is specifically degraded by heat shock can result. Several contradictory descriptions of PABP may also be related to its proteolysis. Repression of proteolysis is likely to reflect a physiologically significant regulatory event, based on recent examinations of HSP70 stability during and after heat shock.

摘要

多聚腺苷酸结合蛋白(PABP)在果蝇组织培养细胞的细胞裂解过程中极易受到蛋白水解作用的影响,除非在提取缓冲液中加入大量的蛋白酶抑制剂。在热休克期间,这种内在的蛋白水解活性会大幅降低。这可能导致多聚腺苷酸结合蛋白被热休克特异性降解的假象。对PABP的一些相互矛盾的描述也可能与其蛋白水解有关。基于最近对热休克期间和之后HSP70稳定性的研究,蛋白酶解的抑制可能反映了一个具有生理意义的调控事件。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d7d/308042/9eb07e787551/nar00033-0139-a.jpg

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