کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1934892 | 1050652 | 2008 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Tyrosine kinase activity of a Ca2+/calmodulin-dependent protein kinase II catalytic fragment
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
CaMKBSA - BSACa2+/calmodulin-dependent protein kinase II - Ca2 + / calmodulin وابسته پروتئین کیناز IIbovine serum albumin - آلبومین سرم گاوAutophosphorylation - اتوفسفورلاسیونSubstrate specificity - خصوصیات زیربناییProtein phosphorylation - فسفوریلاسیون پروتئینIntramolecular reaction - واکنش داخل مولکولیCa2+/calmodulin-dependent protein kinase - پروتئین کیناز وابسته به کلسیم و پتاسیم Ca2 + /
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
A 30-kDa fragment of Ca2+/calmodulin-dependent protein kinase II (30K-CaMKII) is a constitutively active protein Ser/Thr kinase devoid of autophosphorylation activity. We have produced a chimeric enzyme of 30K-CaMKII (designated CX40-30K-CaMKII), in which the N-terminal 40 amino acids of Xenopus Ca2+/calmodulin-dependent protein kinase I (CX40) were fused to the N-terminal end of 30K-CaMKII. Although CX40-30K-CaMKII exhibited essentially the same substrate specificity as 30K-CaMKII, it underwent significant autophosphorylation. Surprisingly, its autophosphorylation site was found to be Tyr-18 within the N-terminal CX40 region of the fusion protein, although it did not show any Tyr kinase activity toward exogenous substrates. Several lines of evidence suggested that the autophosphorylation occurred via an intramolecular mechanism. These data suggest that even typical Ser/Thr kinases such as 30K-CaMKII can phosphorylate Tyr residues under certain conditions. The possible mechanism of the Tyr residue autophosphorylation is discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 377, Issue 2, 12 December 2008, Pages 648-652
Journal: Biochemical and Biophysical Research Communications - Volume 377, Issue 2, 12 December 2008, Pages 648-652
نویسندگان
Yasunori Sugiyama, Atsuhiko Ishida, Noriyuki Sueyoshi, Isamu Kameshita,