scholarly journals 2P169 Molecular interaction between two troponin C and four troponin I of Caenorhabditis elegans

2005 ◽  
Vol 45 (supplement) ◽  
pp. S162
Author(s):  
Ziaul Amin ◽  
Razia Ruksana ◽  
T. Takaya ◽  
H. Kagawa
Keyword(s):  
Caenorhabditis Elegans ◽  
Molecular Interaction ◽  
Troponin I ◽  
Troponin C

scholarly journals Genomic Organization, Expression, and Analysis of the Troponin C Gene pat-10 of Caenorhabditis elegans

1999 ◽  
Vol 146 (1) ◽  
pp. 193-202 ◽  
Author(s):  
Hiromi Terami ◽  
Benjamin D. Williams ◽  
Shin-ichi Kitamura ◽  
Yasuji Sakube ◽  
Shinji Matsumoto ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Calcium Binding ◽  
Troponin I ◽  
Amino Acid Level ◽  
Troponin C ◽  
In Vivo Studies ◽  
Calcium Binding Site ◽  
Expression Studies ◽  
Missense Alteration

We have cloned and characterized the troponin C gene, pat-10 of the nematode Caenorhabditis elegans. At the amino acid level nematode troponin C is most similar to troponin C of Drosophila (45% identity) and cardiac troponin C of vertebrates. Expression studies demonstrate that this troponin is expressed in body wall muscle throughout the life of the animal. Later, vulval muscles and anal muscles also express this troponin C isoform. The structural gene for this troponin is pat-10 and mutations in this gene lead to animals that arrest as twofold paralyzed embryos late in development. We have sequenced two of the mutations in pat-10 and both had identical two mutations in the gene; one changes D64 to N and the other changes W153 to a termination site. The missense alteration affects a calcium-binding site and eliminates calcium binding, whereas the second mutation eliminates binding to troponin I. These combined biochemical and in vivo studies of mutant animals demonstrate that this troponin is essential for proper muscle function during development.

scholarly journals Interaction between Troponin C and Troponin I of body wall in Caenorhabditis elegans

2003 ◽  
Vol 43 (supplement) ◽  
pp. S122
Author(s):  
M. Soda ◽  
T. Takaya ◽  
H. Kagawa ◽  
T. Iio
Keyword(s):  
Caenorhabditis Elegans ◽  
Body Wall ◽  
Troponin I ◽  
Troponin C

scholarly journals Analysis of the Ca^-dependent troponin I binding to the mutagenized troponin C of Caenorhabditis elegans

2003 ◽  
Vol 43 (supplement) ◽  
pp. S121
Author(s):  
T. Takaya ◽  
H. Terami ◽  
H. Kagawa
Keyword(s):  
Caenorhabditis Elegans ◽  
Troponin I ◽  
Troponin C

scholarly journals 1E1430 Molecular interactions of tissue specific isoforms between Troponin I and Troponin C in Caenorhabditis elegans

2002 ◽  
Vol 42 (supplement2) ◽  
pp. S32
Author(s):  
Razia Ruksana ◽  
H. Terami ◽  
Y. Sakube ◽  
H. Kagawa
Keyword(s):  
Caenorhabditis Elegans ◽  
Molecular Interactions ◽  
Troponin I ◽  
Troponin C ◽  
Tissue Specific

scholarly journals A Region of the Myosin Rod Important for Interaction With Paramyosin in Caenorhabditis elegans Striated Muscle

Genetics ◽  
2000 ◽  
Vol 156 (2) ◽  
pp. 631-643
Author(s):  
Pamela E Hoppe ◽  
Robert H Waterston
Keyword(s):  
Caenorhabditis Elegans ◽  
Heavy Chain ◽  
Molecular Interaction ◽  
Striated Muscle ◽  
Genetic Interaction ◽  
Specific Interaction ◽  
Thick Filament ◽  
Parallel Arrangement ◽  
Myosin Rod

Abstract The precise arrangement of molecules within the thick filament, as well as the mechanisms by which this arrangement is specified, remains unclear. In this article, we have exploited a unique genetic interaction between one isoform of myosin heavy chain (MHC) and paramyosin in Caenorhabditis elegans to probe the molecular interaction between MHC and paramyosin in vivo. Using chimeric myosin constructs, we have defined a 322-residue region of the MHC A rod critical for suppression of the structural and motility defects associated with the unc-15(e73) allele. Chimeric constructs lacking this region of MHC A either fail to suppress, or act as dominant enhancers of, the e73 phenotype. Although the 322-residue region is required for suppression activity, our data suggest that sequences along the length of the rod also play a role in the isoform-specific interaction between MHC A and paramyosin. Our genetic and cell biological analyses of construct behavior suggest that the 322-residue region of MHC A is important for thick filament stability. We present a model in which this region mediates an avid interaction between MHC A and paramyosin in parallel arrangement in formation of the filament arms.

scholarly journals Biologically important interactions between synthetic peptides of the N-terminal region of troponin I and troponin C.

1992 ◽  
Vol 267 (22) ◽  
pp. 15715-15720
Author(s):  
S.M. Ngai ◽  
R.S. Hodges
Keyword(s):  
Synthetic Peptides ◽  
Troponin I ◽  
Troponin C ◽  
Terminal Region

scholarly journals Cross-linking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I

1991 ◽  
Vol 266 (21) ◽  
pp. 13746-13751
Author(s):  
T. Kobayashi ◽  
T. Tao ◽  
Z. Grabarek ◽  
J. Gergely ◽  
J.H. Collins
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Cross Linking ◽  
Regulatory Domain ◽  
Inhibitory Region
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