Functional consequences of disulfide bond formation in gelsolin

FEBS Letters

Allen, Philip G¹ 

[1] The Division of Experimental Medicine, Department of Medicine, Brigham and Women's Hospital, LMRC 301, 221 Longwood Avenue, Boston MA 02115, USA

关键词: Gelsolin;    Protein structure;    Disulfide bond;    Calcium binding protein;    Actin binding protein;    TRITC-phalloidin;    tetramethylrhodamine isothiocyanate coupled phalloidin;    DTT;    dithiothreitol;    F-actin;    filamentous actin;    G-actin;    monomeric actin;    PIA;    pyrene iodoacetemide;    DACM;    7-dimethylamino-4-methyl-(N-maleimidyl) coumarin;    n-HPG;    native human plasma gelsolin;    r-HPG;    bacterially expressed human plasma gelsolin lacking the disulfide bond in domain 2;    ox-r-HPG;    bacterially expressed human plasma gelsolin containing the disulfide bond in domain 2;   

DOI  :  10.1016/S0014-5793(96)01439-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Gelsolin is an actin monomer binding and filament severing protein synthesized in plasma and cytoplasmic forms differing by an N-terminal amino acid extension and a disulfide bond between Cys-188 and Cys-201. To determine whether this bond altered gelsolin regulation or function, oxidized and reduced plasma gelsolins were assayed for severing, monomer binding and nucleation activity at a variety of rate-limiting calcium concentrations. The results indicate that the disulfide bond in domain 2 of gelsolin influences the transmission of information from C-terminal regulatory sites to functional sites in the N-terminus.

【 授权许可】

Unknown