کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10766820 | 1050679 | 2008 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Thiol reactivity as a sensor of rotation of the converter in myosin
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کلمات کلیدی
N-ethylmaleimideCa2+-regulationMLCKHMMMDENTMELCRLCheavy meromyosin - meromyosin سنگینAEDANS - آیدانContraction - اختصارThiol modification - اصلاح تیولmotor domain - دامنه موتورessential light chain - زنجیره ای ضروری ضروری استregulatory light chain - زنجیره سبک قانونیmyosin light chain kinase - زنجیره کیناز سبک مایوسینsubfragment-1 - زیرمجموعه 1Phosphorylation - فسفریلاسیونsmooth muscle myosin - میوزین عضله صافNEM - نهIAEDANS - یادانس
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Smooth muscle myosin has two reactive thiols located near the C-terminal region of its motor domain, the “converter”, which rotates by â¼70° upon the transition from the “nucleotide-free” state to the “pre-power stroke” state. The incorporation rates of a thiol reagent, 5-(((2-iodoacetyl)amino)ethyl)aminonaphthalene-1-sulfonic acid (IAEDANS), into these thiols were greatly altered by adding ATP or changing the myosin conformation. Comparisons of the myosin structures in the pre-power stroke state and the nucleotide-free state explained why the reactivity of both thiols is especially sensitive to a conformational change around the converter, and thus can be used as a sensor of the rotation of the converter. Modeling of the myosin structure in the pre-power stroke state, in which the most reactive thiol, “SH1”, was selectively modified with IAEDANS, revealed that this label becomes an obstacle when the converter completely rotates toward its position in the pre-power stroke state, thus resulting in incomplete rotation of the converter. Therefore, we suggest that the limitation of the converter rotation by modification causes the as-yet unexplained phenomena of SH1-modified myosin, including the inhibition of 10S myosin formation and the losses in phosphorylation-dependent regulation of the basic and actin-activated Mg-ATPase activities of myosin.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 369, Issue 1, 25 April 2008, Pages 115-123
Journal: Biochemical and Biophysical Research Communications - Volume 369, Issue 1, 25 April 2008, Pages 115-123
نویسندگان
Hirofumi Onishi, Yasushi Nitanai,