Investigation of a genetically engineered mutant of barnacle troponin C containing a central helix deletion

1999 ◽  
Vol 439 (1-2) ◽  
pp. 67-75 ◽  
Author(s):  
Allhouse L. ◽  
T. Miller ◽  
Q. Li ◽  
G. Guzman ◽  
Potter J. ◽  
...  
1999 ◽  
Vol 439 (1) ◽  
pp. 67-75
Author(s):  
L. Allhouse ◽  
T. Miller ◽  
Q. Li ◽  
G. Guzman ◽  
J. Potter ◽  
...  

FEBS Letters ◽  
1994 ◽  
Vol 354 (2) ◽  
pp. 135-139 ◽  
Author(s):  
David Keleti ◽  
Venu G. Rao ◽  
Hong Su ◽  
Arvind B. Akella ◽  
Xiao-Ling Ding ◽  
...  

Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15515-15521 ◽  
Author(s):  
Sundaram Ramakrishnan ◽  
Sarah E. Hitchcock-DeGregori

2002 ◽  
Vol 34 (6) ◽  
pp. 657-667 ◽  
Author(s):  
Elizabeth F. da Silva ◽  
Vanessa H. Oliveira ◽  
Martha M. Sorenson ◽  
Hector Barrabin ◽  
Helena M. Scofano
Keyword(s):  

1991 ◽  
Vol 266 (9) ◽  
pp. 5703-5710
Author(s):  
Z Dobrowolski ◽  
G Q Xu ◽  
S E Hitchcock-DeGregori

Biochemistry ◽  
1991 ◽  
Vol 30 (29) ◽  
pp. 7089-7096 ◽  
Author(s):  
Zbigniew Dobrowolski ◽  
Gong Qiao Xu ◽  
Wei Chen ◽  
Sarah E. Hitchcock-DeGregori

1997 ◽  
Vol 321 (3) ◽  
pp. 873-878 ◽  
Author(s):  
Alexei A. POLYAKOV ◽  
Nikolai B. GUSEV

Troponin C, a structural analogue of calmodulin, was used for mapping the calmodulin-binding sites of caldesmon. The apparent Kd values for the formation of the caldesmonŐcalcium-binding-protein complex as determined by native gel electrophoresis were 0.5, 1.2 and 3.9 ƁM for calmodulin, rabbit skeletal muscle troponin C and bovine cardiac troponin C respectively. Troponin C induced a 4Ő6 nm blue shift of the Trp fluorescence of caldesmon without affecting the amplitude of fluorescence. In the presence of Ca2+, troponin C induced partial displacement of caldesmon from actinŐtropomyosin complexes. Addition of 5,5ƀ-dithiobis(nitrobenzoic) acid to an equimolar complex of caldesmon and troponin C induced disulphide cross-linking between Cys-98 of rabbit skeletal muscle troponin C and the single Cys residue of duck gizzard caldesmon, located in a position analogous to Cys-580 of the chicken gizzard protein. The cross-linked caldesmonŐtroponin C complex was ineffective in inhibiting actomyosin ATPase activity. It is concluded that Cys-580 of caldesmon can be located close to both the central helix of calcium-binding proteins and the C-terminal domain of actin. This may be important for the regulation of actomyosin ATPase activity by caldesmon.


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