Importance of the ATP-binding domain and nucleolar localization domain of HSP72 in the protection of nuclear proteins against heat-induced aggregation Journal Article
| Authors: | Stege, G. J. J.; Li, L.; Kampinga, H. H.; Konings, A. W. T.; Li, G. C. |
| Article Title: | Importance of the ATP-binding domain and nucleolar localization domain of HSP72 in the protection of nuclear proteins against heat-induced aggregation |
| Abstract: | Heat treatment of cells results in an increased protein content of nuclei when isolated after the heat treatment (intranuclear protein aggregation). In a previous study, the role of HSP72 was using Rat-1 fibroblasts stably transfected with the human HSP72 gene. It was observed that the expression of human HSP72 in Rat-1 cells (HR cells) confers heat resistance. The initial heat-induced increase in the nuclear protein content was lower in HR cells as compared to the parent Rat-1 cells. In the present communication, the effects of overexpression of intact or mutant human HSP72 in Rat-1 cells on heat-induced increase in intranuclear protein aggregation and their relationship to cells' thermal sensitivity were examined. Four closely related cell lines were used for this study: Rat-1 cells which constitutively expressed the intact human HSP72, or mutant human HSP72 either missing its ATP-binding domain or nucleolar localization domain, and wild type Rat-1 cells. Our results show that expression of the intact human HSP72 or mutant human HSP72 missing its ATP-binding domain confers heat resistance and protects cells against heat-induced intranuclear protein aggregation. On the other hand, cells expressing mutant human HSP72 missing its nucleolar localization domain demonstrated heat shock responses similar to control Rat-1 cells. © 1994 Academic Press, Inc. |
| Journal Title: | Experimental Cell Research |
| Volume: | 214 |
| Issue: | 1 |
| ISSN: | 0014-4827 |
| Publisher: | Elsevier Inc. |
| Date Published: | 1994-09-01 |
| Start Page: | 279 |
| End Page: | 284 |
| Language: | English |
| DOI: | 10.1006/excr.1994.1259 |
| PROVIDER: | scopus |
| PUBMED: | 8082731 |
| DOI/URL: | |
| Notes: | Export Date: 14 January 2019 -- Article -- Source: Scopus |
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