On the mode of alkali light chain association to the heavy chain of myosin subfragment 1. Evidence for the involvement of the carboxyl-terminal region of the heavy chain

Biochemistry ◽  
1983 ◽  
Vol 22 (13) ◽  
pp. 3046-3053 ◽  
Author(s):  
Morris Burke ◽  
Mathoor Sivaramakrishnan ◽  
Vedhachalam Kamalakannan
1992 ◽  
Vol 284 (1) ◽  
pp. 75-79 ◽  
Author(s):  
J P Labbé ◽  
M Boyer ◽  
C Roustan ◽  
Y Benyamin

The actin-myosin head complex in the rigor state reveals several high-affinity sites on the actin molecule in sequences 18-28 and 40-113. In the presence of Mg(2+)-ATP, participation of the actin N-terminal 1-7 sequence is known to occur. The proximity of the C-terminal region of actin to the A1 light chain of the myosin head [S-1(A1)] (where S-1 is myosin subfragment-1) was described previously. We observed that C-terminal antigenic structures located near Met-305, Met-325 and Met-355 and the C-terminal end (Cys-374) of actin are markedly modified in the presence of S-1(A1), S-1(A2) and scallop S-1 and in the absence of Mg(2+)-ATP. This seems to rule out any important specific involvement of the A1 light chain in the described conformational changes. An S-1-binding site was located in this actin C-terminal region by testing the tryptic CB9 peptide (360-372 sequence) previously implicated in the A1 light chain interaction. This peptide was able to bind well to S-1(A1), S-1(A2) and scallop S-1, but not in the presence of Mg(2+)-pyrophosphate. These results strengthen the hypothesis of a multisite interface between S-1 and actin located in the actin subdomain I.


Traffic ◽  
2007 ◽  
Vol 8 (8) ◽  
pp. 1101-1110 ◽  
Author(s):  
Joel A. Ybe ◽  
Samantha Perez-Miller ◽  
Qian Niu ◽  
David A. Coates ◽  
Michael W. Drazer ◽  
...  

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