کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10765025 | 1050581 | 2010 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A new property of twitchin to restrict the “rolling” of mussel tropomyosin and decrease its affinity for actin during the actomyosin ATPase cycle
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کلمات کلیدی
DTTEGTApKaIAFethylene glycol-bis (2-aminoethylether)-N,N,N′,N′-tetraacetic acidtroponin complexGhost muscle fibersATPase cycleTwitchinmyosin subfragment-1 - بخش زیر Myosin-1Tropomyosin - تروپومیوسینdithiothreitol - دیتیوتریتولPolarized fluorescence - فلورسانس قطبیcAMP-dependent protein kinase - پروتئین کیناز وابسته به cAMP
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: A new property of twitchin to restrict the “rolling” of mussel tropomyosin and decrease its affinity for actin during the actomyosin ATPase cycle A new property of twitchin to restrict the “rolling” of mussel tropomyosin and decrease its affinity for actin during the actomyosin ATPase cycle](/preview/png/10765025.png)
چکیده انگلیسی
A new evidence on the regulatory function of twitchin, a titin-like protein of molluscan muscles, at muscle contraction has been obtained at studying the movements of IAF-labeled mussel tropomyosin in skeletal ghost fibers during the ATP hydrolysis cycle simulated using nucleotides and non-hydrolysable ATP analogs. For the first time, myosin-induced multistep changes in mobility and in the position of mussel tropomyosin strands on the surface of the thin filament during the ATP hydrolysis cycle have been demonstrated directly. Unphosphorylated twitchin shifts the tropomyosin towards the position typical for muscle relaxation, decreases the tropomyosin affinity to actin and inhibits its movements during the ATPase cycle. Phosphorylation of twitchin by the catalytic subunit of protein kinase A reverses this effect. These data imply that twitchin is a thin filament regulator that controls actin-myosin interaction by “freezing” tropomyosin in the blocked position, resulting in the inhibition of the transformation of weak-binding states into strong-binding ones during ATPase cycle.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 394, Issue 1, 26 March 2010, Pages 126-129
Journal: Biochemical and Biophysical Research Communications - Volume 394, Issue 1, 26 March 2010, Pages 126-129
نویسندگان
Stanislava V. Avrova, Nikolay S. Shelud'ko, Yurii S. Borovikov,