TAILIEUCHUNG - Báo cáo khoa học: Calcium-dependent protein–protein interactions induce changes in proximity relationships of Cys48 and Cys64 in chicken skeletal troponin I

The goal of this study was to relate conformational changes in the N-terminal domain of chicken troponin I (TnI) to Ca 2+ activation of the actin–myosin two cysteine residues in this region (Cys48 and Cys64) were labeled with two sulfhydryl-reactive pyrene-containing fluorophores [N-(1-pyrene)maleimide, and N-(1-pyrene)-iodoacetamide].The labeled TnI showed a typical fluores-cence spectrum: two sharp peaks of monomer fluorescence and a broad peak of excimer fluorescence arising from the formation of an excited dimer (excimer) | Eur. J. Biochem. 270 3092-3100 2003 FEBS 2003 doi Calcium-dependent protein-protein interactions induce changes in proximity relationships of Cys48 and Cys64 in chicken skeletal troponin I Ying-Ming Liou and Ming-Wei Chen Department of Life Science Institute of Biochemistry National Chung-Hsing University Taichung Taiwan The goal of this study was to relate conformational changes in the N-terminal domain of chicken troponin I TnI to Ca2 activation of the actin-myosin interaction. The two cysteine residues in this region Cys48 and Cys64 were labeled with two sulfhydryl-reactive pyrene-containing fluorophores N- 1-pyrene maleimide and N- 1-pyrene -iodoacetamide . Tire labeled Tnl show-ed a ty iical fluorescence spectrum two sharp peaks of monomer fluorescence and a broad peak of excimer fluorescence arising from the formation of an excited dimer excimer . Rsullte ohtanred show that forming a binary complex of labeled TnI with skeletal TnC sTnC in the absence of Ca2 decreases the excimer fluorescence indicating a separation of the two reduction in excimer fluorescence does not occur when labeled TnI is complexed with cardiac TnC cTnC . TSc kitin cuusk OTÚy aaráal ectiaarinn o ì iSc Ca2 -dependent myohbrillar ATPase. The binding of Ca2 to the two N-teaminal sites of sTnC causes a signihcant decrease in excimer fluorescence and an increase in monomer fluorescence in complexes of labeled TnI with skeletal TnC or TnC TnT while Ca2 binding to site II of cTnC only causes an increase in monomer fluorescence but no change in excimer fluoresesnes. Thus a ccmlormaiional change m the N-teaminal region of TnI may be necessary for full activation of muscle contraction. Keywords proximity relationships cysteine residues pyrene-containing fluorophores monomer fluorescence excimer fluorescence. Ca2 activation of striated muscle is mediated by the troponin complex. Troponin is composed of three subunits troponin C TnC a Ca2 binding .

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