Localization of a new proteolytic site accessible in oxidized myosin rod

FEBS Letters

Nyitray, László¹  Mócz, Gábor¹  Bálint, Miklós¹ 

[1] Department of Biochemistry, Eötvös L. University, Puskin u. 3, H-1088 Budapest, Hungary

关键词: Myosin rod;    Coiled-coil structure;    Disulfide crosslinking;    Limited proteolysis;    HMM;    heavy meromyosin;    LMM;    light meromyosin;    S2;    myosin subfragment-2;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    Nbs2;    5;    5'-dithiobis-2-nitrobenzoate;   

DOI  :  10.1016/0014-5793(85)80291-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have compared the proteolysis pattern of reduced and oxidized myosin rods in which the five pairs of SH-groups were interchain crosslinked by employing CuCl₂ or 5,5'-dithiobis-2-nitrobenzoate. In the tryptic digest of oxidized rod three new fragments appeared on SDS-polyacrylamide gel electrophoresis (chain masses of 100, 45, and 25 kDa). Based on the N-terminal sequences of the isolated peptides, it is concluded that oxidation creates a new cleavage site 102 residues away from the N-terminus of the rod, in the vicinity of one of the modified SH-groups (Cys-108). This observation indicates that S-S crosslinking of myosin rod leads to a local unfolding of the coiled-coil structure.

【 授权许可】

Unknown