scholarly journals Characterization of the dextran-binding domain in the glucan-binding protein C of Streptococcus mutans

2015 ◽  
Vol 119 (4) ◽  
pp. 1148-1157 ◽  
Author(s):  
Y. Takashima ◽  
K. Fujita ◽  
A.C. Ardin ◽  
K. Nagayama ◽  
R. Nomura ◽  
...  
Keyword(s):  
Streptococcus Mutans ◽  
Protein C ◽  
Binding Protein ◽  
Binding Domain

The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle

1996 ◽  
Vol 109 (1) ◽  
pp. 101-111 ◽  
Author(s):  
R. Gilbert ◽  
M.G. Kelly ◽  
T. Mikawa ◽  
D.A. Fischman
Keyword(s):  
Amino Acids ◽  
Protein C ◽  
Binding Protein ◽  
Thick Filament ◽  
Binding Domain ◽  
C Protein ◽  
Amino Terminal ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding

Myosin binding protein-C (MyBP-C), also known as C-protein, is a major constituent of the thick filaments of vertebrate striated muscles. The protein, approximately 130 kDa, consists of a series of 10 globular motifs (numbered I to X) each of approximately 90–100 amino acids, bearing resemblance to the C2-set of immunoglobins (Ig C2) and to the fibronectin type III (FnIII) motifs. Using pure preparations of myosin and MyBP-C, it has been demonstrated that the major myosin binding domain of MyBP-C resides within the C-terminal Ig C2 motif (motif X). However, in the context of the in vivo thick filament, it is uncertain if the latter domain is sufficient to target MyBP-C correctly to the A-band or if other regions of the molecule are required for this process. To answer this question, cultures of skeletal muscle myoblasts were transfected with expression plasmids encoding seven truncation mutants of MyBP-C, and their targeting to the A-band investigated by immunofluorescence microscopy. To distinguish the recombinant proteins from endogenous MyBP-C, a myc epitope was inserted at each amino terminus. Recombinant MyBP-C exhibited an identical distribution in the sarcomere to that of native MyBP-C; i.e. it was found exclusively in the C-zone of the A-band. A mutant encoding the C-terminal 372 amino acids, but lacking motifs I-VI (termed delta 1–6), also targeted correctly to the A-band. This fragment, which is composed of two Ig C2 and two FnIII motifs, was the minimal protein fragment required for correct A-band incorporation. Larger amino-terminal deletions or deletion of motif X, the myosin binding domain, abolished all localization to the A-band. One construct (delta 10) lacking only motif X strongly inhibited myofibril assembly. We conclude that the myosin binding domain of MyBP-C, although essential, is not sufficient for correct incorporation into the A-band and that motifs VII to IX are required for this process. The data suggest a topological model in which MyBP-C is associated with the thick filament through its C terminus.

scholarly journals Identification and characterization of amylase-binding protein C fromStreptococcus mitisNS51

2010 ◽  
Vol 25 (2) ◽  
pp. 150-156 ◽  
Author(s):  
J. Vorrasi ◽  
B. Chaudhuri ◽  
E.M. Haase ◽  
F.A. Scannapieco
Keyword(s):  
Protein C ◽  
Binding Protein ◽  
Identification And Characterization

Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans

2012 ◽  
Vol 27 (4) ◽  
pp. 308-323 ◽  
Author(s):  
R. Nomura ◽  
K. Nakano ◽  
S. Naka ◽  
H. Nemoto ◽  
K. Masuda ◽  
...  
Keyword(s):  
Streptococcus Mutans ◽  
Binding Protein ◽  
Collagen Binding ◽  
Identification And Characterization

scholarly journals Characterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A.

1993 ◽  
Vol 175 (18) ◽  
pp. 5762-5768 ◽  
Author(s):  
M A Goldstein ◽  
M Takagi ◽  
S Hashida ◽  
O Shoseyov ◽  
R H Doi ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Clostridium Cellulovorans ◽  
Cellulose Binding
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