Cross-linking of the 25- and 20-kilodalton fragments of skeletal myosin subfragment-1 by a bifunctional ATP analog

Biochemistry ◽  
1990 ◽  
Vol 29 (42) ◽  
pp. 9910-9915 ◽  
Author(s):  
Shinsaku Maruta ◽  
Morris Burke ◽  
Mitsuo Ikebe
Keyword(s):  
Cross Linking ◽  
Myosin Subfragment ◽  
Skeletal Myosin ◽  
Myosin Subfragment 1

Specific cross-linking of the SH1 thiol of skeletal myosin subfragment 1 to F-actin and G-actin

Biochemistry ◽  
1992 ◽  
Vol 31 (2) ◽  
pp. 389-395 ◽  
Author(s):  
Nadir Bettache ◽  
Raoul Bertrand ◽  
Ridha Kassab
Keyword(s):  
Cross Linking ◽  
Myosin Subfragment ◽  
Skeletal Myosin ◽  
Myosin Subfragment 1

scholarly journals Involvement of caldesmon at the actin-myosin interface

1992 ◽  
Vol 287 (2) ◽  
pp. 633-637 ◽  
Author(s):  
M C Harricane ◽  
E Fabbrizio ◽  
C Arpin ◽  
D Mornet
Keyword(s):  
Ternary Complex ◽  
Actin Binding ◽  
Cross Linking ◽  
Binary Complex ◽  
Binding Region ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Spacer Arm ◽  
Protein Components ◽  
Chemical Cross Linking

Addition of myosin subfragment 1 (S-1) to the actin-caldesmon binary complex, which forms bundles of actin filaments resulted in the formation of actin/caldesmon-decorated filaments [Harricane, Bonet-Kerrache, Cavadore & Mornet (1991) Eur. J. Biochem. 196, 219-224]. The present data provide further evidence that caldesmon and S-1 compete for a common actin-binding region and demonstrate that a change occurs in the actin-myosin interface induced by caldesmon. S-1 digested by trypsin, which has an actin affinity 100-fold weaker than that of native S-1, was efficiently removed from actin by caldesmon, but not completely dissociated. This particular ternary complex was stabilized by chemical cross-linking with carbodi-imide, which does not have any spacer arm, and revealed contact interfaces between the different protein components. Cross-linking experiments showed that the presence of caldesmon had no effect on stabilization of actin-(20 kDa domain), whereas the actin-(50 kDa domain) covalent association was significantly decreased, to the point of being virtually abolished.

Tryptophan-130 is the most reactive tryptophan residue in rabbit skeletal myosin subfragment-1

FEBS Letters ◽  
1990 ◽  
Vol 259 (2) ◽  
pp. 346-348 ◽  
Author(s):  
Y.Michael Peyser ◽  
Andras Muhlrad ◽  
Moshe M. Werber
Keyword(s):  
Tryptophan Residue ◽  
Myosin Subfragment ◽  
Skeletal Myosin ◽  
Myosin Subfragment 1
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