Submitted on August 23, 2007
Accepted on October 15, 2007
Functional and Evolutionary Relationships of Troponin C
Todd E. Gillis1*, Christian R Marshall2, and Glen F. Tibbits3
1 Integrative Biology, University of Guelph, Guelph, Canada
2 The Centre for Applied Genomics, Hospital For Sick Children, Toronto, Canada
3 Cardiac Membrane Research Laboratory, Simon Fraser University, Burnaby, Canada; Cardiovascular Sciences, Child & Family Research Institute, Vancouver, BC, Canada
* To whom correspondence should be addressed. E-mail: tgillis{at}uoguelph.ca.
Striated muscle contraction is initiated when, following membrane depolarization, Ca2+ binds to the low affinity Ca2+ binding sites of troponin C (TnC). The Ca2+ activation of this protein results in a rearrangement of the components (troponin I, troponin T, and tropomyosin) of the thin filament resulting in increased interaction between actin and myosin and the formation of cross-bridges. The functional properties of this protein are therefore critical in determining the active properties of striated muscle. To date there are 61 known TnCs that have been cloned from 41 vertebrate and invertebrate species. In vertebrate species there are also distinct fast skeletal muscle and cardiac TnC proteins. While there is relatively high conservation of the amino acid sequence of TnC homologs between species and tissue types there is wide variation in the functional properties of these proteins. To date there has been extensive study of the structure and function of this protein and how differences in these translate into the functional properties of muscles. The purpose of this work is to integrate these studies of TnC with phylogenetic analysis to investigate how changes in the sequence and function of this protein, integrate with the evolution of striated muscle.
