Rabbit skeletal muscle myosin unfolded carboxyl‐terminus and its role in molecular assembly

FEBS Letters

Rösch, Andrea¹  Maeda, Kayo¹  Maéda, Yuichiro²  Kalbitzer, Hans Robert¹  Wittinghofer, Alfred¹ 

[1] Max-Planck-Institut für medizinische Forschung, Jahnstraße 29, W-6900 Heidelberg, Germany;European Molecular Biology Laboratory at DESY, Notkestraße 85, W-2000 Hamburg 52, Germany

关键词: Myosin;    α-Helical coiled-coil;    Self-assembly;    Recombinant DNA technique;    Nuclear magnetic resonance;    LMM;    light meromyosin;    NMR;    nuclear magnetic resonance;   

DOI  :  10.1016/0014-5793(91)80349-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have expressed in E. coli segments of the rod portion of rabbit skeletal fast muscle myosin and compared physical properties of two different species, LMM-30 and LMM-30C′. LMM-30 consists of 263 amino acids including the original C-terminus of myosin heavy chain. LMM-30C′ is colinear with LMM-30, but is devoid of 17 residues at the C-terminus. ¹H NMR spectroscopy indicates that the C-terminus of LMM-30, but not of LMM30C′ is unfolded and freely mobile. Furthermore, the present results show that the unfolded C-terminus is essential for molecular assembly of LMM-30; at pH 8.0 LMM-30, but not LMM-30C′, formed aggregates upon decreasing the ionic strength.

【 授权许可】

Unknown