scholarly journals Chemical Cross-linking of Actin and Myosin Subfragment-1 in Rigor Complex

10.5109/4571 ◽  
2004 ◽  
Vol 49 (1) ◽  
pp. 111-118
Author(s):  
Ken Jyh-Fang Liaw ◽  
Sunao Mori ◽  
Sumie Hasimoto ◽  
Miyako Sugimitsu ◽  
Minoru Yamanoue ◽  
...  
Keyword(s):  
Cross Linking ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Chemical Cross Linking

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.

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 Cross-linking of myosin subfragment 1. Nucleotide-enhanced modification by a variety of bifunctional reagents.

1980 ◽  
Vol 255 (23) ◽  
pp. 11135-11140
Author(s):  
J.A. Wells ◽  
C. Knoeber ◽  
M.C. Sheldon ◽  
M.M. Werber ◽  
R.G. Yount
Keyword(s):  
Cross Linking ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

scholarly journals Transglutaminase-Induced Cross-Linking between Subdomain 2 of G-Actin and the 636–642 Lysine-Rich Loop of Myosin Subfragment 1

1998 ◽  
Vol 74 (2) ◽  
pp. 953-963 ◽  
Author(s):  
Luba Eligula ◽  
Li Chuang ◽  
Martin L. Phillips ◽  
Masao Motoki ◽  
Katsuya Seguro ◽  
...  
Keyword(s):  
Cross Linking ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1
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