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A more recent version of this article appeared on April 27, 2001
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Papers In Press, published online ahead of print February 5, 2001
J. Biol. Chem, 10.1074/jbc.M011476200
Submitted on December 20, 2000
Revised on January 31, 2001
Accepted on February 2, 2001

The heme-regulated eIF2alpha kinase: A potential regulatory target for control of protein synthesis by diffusible gases

Sheri Uma, Bo-Geon Yun, and Robert L. Matts

Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078-3035

Corresponding Author: rmatts{at}biochem.okstate.edu

Nitric oxide (NO) has been reported to inhibit protein synthesis in eukaryotic cells by increasing the phosphorylation of the alpha -subunit of eukaryotic initiation factor eIF2. However, the mechanism through which this increase occurs has not been characterized. In this report, we examined the effect of the diffusible gases nitric oxide (NO) and carbon monoxide (CO) on the activation of the heme-regulated eIF2alpha kinase (HRI) in rabbit reticulocyte lysate. Spectral analysis indicated that both NO and CO bind to the N-terminal heme-binding domain (NT-HBD) of HRI. While NO was a very potent activator of HRI, CO markedly suppressed NO-induced HRI activation. The NO-induced activation of HRI was transduced through the interaction of NO with the NT-HBD of HRI and not through S-nitrosylation of HRI. We postulate that the regulation of HRI activity by diffusible gases may be of wider physiological significance, as we further demonstrate that NO-generators increase eIF2alpha phosphorylation levels in NT2 neuroepithelial and C2C12 myoblast cells and activates HRI immunoadsorbed from extracts of these non-erythroid cells lines.


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