Structural Interactions Responsible for the Assembly of the Troponin Complex on the Muscle Thin Filament

Cell Structure and Function

Patricia B. Monteiro¹  Fernando C. Reinach¹  Bettina Malnic¹  Chuck S. Farah¹ 

[1] Dept. Bioquimica, Inst. de Quimica, University of São Paulo

关键词: Caenorhabditis elegaas;    tropomyosin;    troponin C;    muscle development;    levamisole;   

DOI  :  10.1247/csf.22.219

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(30)Cited-By(6)Skeletal muscle contraction is regulated by a complex of five polypeptides which are stably associated with the actin filament. This complex consists of two proteins: troponin with three subunits (TnC; TnI and TnT) and tropomyosin (a dimer of two chains). Using deletion mutants of TnC, TnI and TnT we determined that each of these polypeptides can be divided into at least two domains. One domain is responsible for the regulatory properties of the protein. Its interaction with the other components of the system change upon calcium binding to TnC. A second domain present in each of these proteins is responsible for the stable association of the complex to the actin filament. The interactions among this second set of domains is not influenced by calcium binding to TnC. The structural interactions are: 1) interactions between the C-domain of TnC with the N-domain of TnI; 2) interactions of the N-domain of TnI with the C-terminal domain of TnT and 3) interactions between the N-domain of TnT (T1) and actin/tropomyosin.

【 授权许可】

Unknown