NDLI: Hsp90 regulates protein synthesis by activating the heme-regulated eukaryotic initiation factor 2α (eIF-2α) kinase in rabbit reticulocyte lysates

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Journal of Biosciences : Volume 23, Issue 3, September 1998

Journal of Biosciences : Volume 23, Issue 2, June 1998

Journal of Biosciences : Volume 23, Issue 1, March 1998

Journal of Biosciences : Volume 22

Hsp90 regulates protein synthesis by activating the heme-regulated eukaryotic initiation factor 2α (eIF-2α) kinase in rabbit reticulocyte lysates

Content Provider	Springer Nature Link
Author	Pal, Jayanta K
Copyright Year	1998
Abstract	Heat shock protein 90 (Hsp90), an abundant and ubiquitous cytoplasmic protein has recently been indicated to participate in the regulation of protein synthesis by interacting with the heme-regulated eukaryotic initiation factor 2α (eIF-2α) kinase, also known as the heme-regulated inhibitor (HRI). However, there exists an ambiguity on the exact nature of its action. In this investigation, the interaction of Hsp90 and HRI has been examined bothin vitro using purified proteins, andin situ in rabbit reticulocyte lysates subjected to heat shock and treatment with N-ethylmaleimide (NEM), a sulfhydryl reagent known to induce stress response. During heat shock or NEM-treatment of reticulocyte lysates, Hsp90 co-immunoprecipitated with activated HRI by anti-HRI monoclonal antibodies. Furthermore, the amount of Hsp90 being associated with HRI was a function of duration of heat shock and was correlated with the extent of HRI activation. Interestingly, simultaneous heat shock and NRM-treatment of reticulocyte lysates led to maximal association of HRI and Hsp90, leaving nearly no free HRI in the lysates.In vitro, with the purified proteins, the autokinase and the eIF-2α kinase activities of HRI were enhanced when HRI was pre-incubated with Hsp90, both in the presence and absence of hemin. These data, therefore, clearly demonstrate that Hsp90 interacts with HRI during stress, and that this association leads to activation of HRI and thereby inhibition of protein synthesis at the level of initiation. Considering the ubiquitous nature of Hsp90 and the presence of HRI or HRI-like eIF-2α kinase activity in a number of organisms, it is highly possible that Hsp90 may universally mediate down regulation of global protein synthesis during stress response.
Starting Page	353
Ending Page	360
Page Count	8
File Format	PDF
ISSN	02505991
Journal	Journal of Biosciences
Volume Number	23
Issue Number	4
e-ISSN	09737138
Language	English
Publisher	Springer India
Publisher Date	1998-01-01
Publisher Institution	Indian Academy of Sciences
Publisher Place	New Delhi
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Hsp90 HRI heat shock NEM-activation co-immunoprecipitation protein synthesis Life Sciences Biomedicine general Zoology Plant Sciences Microbiology Cell Biology
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry, Genetics and Molecular Biology Agricultural and Biological Sciences

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