کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10801037 | 1054724 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interdomain interactions regulate the activation of the heme-regulated eIF2α kinase
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
The heme-regulated inhibitor of protein synthesis (HRI) regulates translation through the phosphorylation of the α-subunit of eukaryotic initiation factor-2 (eIF2). While HRI is best known for its activation in response to heme-deficiency, we recently showed that the binding of NO and CO to the N-terminal heme-binding domain (NT-HBD) of HRI activated and suppressed its activity, respectively. Here, we examined the effect of hemin, NO, and CO on the interaction between the NT-HBD and the catalytic domain of HRI (HRI/ÎHBD). Hemin stabilized the interaction of NT-HBD with HRI/ÎHBD, and NO and CO disrupted and stabilized this interaction, respectively. Mutant HRI (ÎH-HRI), lacking amino acids 116-158 from the NT-HBD, was less sensitive to heme-induced inhibition, and mutant NT-HBD lacking these residues did not bind to HRI/ÎHBD. HRI/ÎHBD and ÎH-HRI also activated more readily than HRI in response to heme-deficiency. Thus, HRI's activity is regulated through the modulation of the interaction between its NT-HBD and catalytic domain.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1725, Issue 2, 15 September 2005, Pages 174-181
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1725, Issue 2, 15 September 2005, Pages 174-181
نویسندگان
Bo-Geon Yun, Jessica A.B. Matts, Robert L. Matts,