Heat shock protein hsp70 protects cells from thermal stress even after deletion of its ATP-binding domain Journal Article


Authors: Li, G. C.; Li, L.; Liu, R. Y.; Rehman, M.; Lee, W. M. F.
Article Title: Heat shock protein hsp70 protects cells from thermal stress even after deletion of its ATP-binding domain
Abstract: Retroviral-mediated gene transfer experiments show that rodent cells become heat resistant when stably and constitutively expressing a cloned human gene encoding an intact human 70-kDa heat shock protein (hsp70). Cells expressing higher levels of the hsp70 protein generally tolerate thermal stress better, whereas cells expressing either of two mutated hsp70-encoding genes, one with a 4-base pair out-of-frame. deletion and one with an in-frame deletion of codons 438-618, are heat sensitive. These results provide strong evidence that expression of hsp70 leads directly to thermal tolerance. Surprisingly, cells expressing a mutant hsp70 of a human gene missing codons 120-428 are, nevertheless, heat resistant. Because the deleted region of this mutant contains the ATP-binding domain of human hsp70, this domain appears dispensable in the hsp70-mediated protection of cells from thermal stress.
Keywords: gene; retrovirus; thermotolerance; stable expression; expression; induction; recovery; localization; construction; atp binding; chinese-hamster fibroblasts; resistant variants; thermal resistance
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 89
Issue: 6
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1992-03-15
Start Page: 2036
End Page: 2040
Language: English
ACCESSION: WOS:A1992HJ05300009
DOI: 10.1073/pnas.89.6.2036
PROVIDER: wos
PMCID: PMC48591
PUBMED: 1549562
Notes: Article -- Source: Wos
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  1. Ligeng Li
    21 Li
  2. Gloria C Li
    132 Li