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Effect of temperature on the structure of trout troponin C.

Blumenschein TM, Gillis TE, Tibbits GF, Sykes BD
Biochemistry 43 4955-63 (2004)
Cited: 15 times
EuropePMC logo PMID: 15109253

Abstract

Adaptation for life at different temperatures can cause changes in many aspects of an organism. One example is the expression of different protein isoforms in species adapted to different temperatures. The calcium regulatory protein cardiac troponin C (cTnC), from rainbow trout (Oncorhynchus mykiss), is a good model for studying temperature effects, both because of its low physiological temperature and because mammalian cTnC, extensively studied at higher temperatures, can be used for comparison. We determined the structure and studied the backbone dynamics of the regulatory domain of trout cardiac troponin C (ScNTnC) with one Ca(2+) bound at 7 and 30 degrees C, using nuclear magnetic resonance spectroscopy (NMR). The overall fold of the regulatory domain of trout cTnC at both temperatures is similar to the regulatory domain of mammalian (human, bovine, and porcine isoform) cTnC bound to one Ca(2+). By comparing the trout structures at the two temperatures, we identify differences between the positions of the helices flanking the calcium binding loops, and the overall structure at 7 degrees C is more compact than that at 30 degrees C. The structure at 7 degrees C is more similar to the mammalian cTnC, which was determined at 30 degrees C, indicating that they have the same conformation at their respective physiological temperatures. The dynamic properties of the regulatory domain of trout cTnC are similar at the two temperatures that were used in these studies.

Articles - 1r2u mentioned but not cited (2)

  1. Characterization of Zebrafish Cardiac and Slow Skeletal Troponin C Paralogs by MD Simulation and ITC. Stevens CM, Rayani K, Genge CE, Singh G, Liang B, Roller JM, Li C, Li AY, Tieleman DP, van Petegem F, Tibbits GF. Biophys J 111 38-49 (2016)
  2. The structural and functional effects of the familial hypertrophic cardiomyopathy-linked cardiac troponin C mutation, L29Q. Robertson IM, Sevrieva I, Li MX, Irving M, Sun YB, Sykes BD. J Mol Cell Cardiol 87 257-269 (2015)


Reviews citing this publication (4)

  1. Functional and evolutionary relationships of troponin C. Gillis TE, Marshall CR, Tibbits GF. Physiol Genomics 32 16-27 (2007)
  2. Temperature-induced cardiac remodelling in fish. Keen AN, Klaiman JM, Shiels HA, Gillis TE. J Exp Biol 220 147-160 (2017)
  3. Cardiac Troponin and Tropomyosin: Structural and Cellular Perspectives to Unveil the Hypertrophic Cardiomyopathy Phenotype. Marques MA, de Oliveira GA. Front Physiol 7 429 (2016)
  4. The missing links within troponin. Marques MA, Parvatiyar MS, Yang W, de Oliveira GAP, Pinto JR. Arch Biochem Biophys 663 95-100 (2019)

Articles citing this publication (9)

  1. Familial hypertrophic cardiomyopathy-related cardiac troponin C mutation L29Q affects Ca2+ binding and myofilament contractility. Liang B, Chung F, Qu Y, Pavlov D, Gillis TE, Tikunova SB, Davis JP, Tibbits GF. Physiol Genomics 33 257-266 (2008)
  2. Modulation of cardiac troponin C function by the cardiac-specific N-terminus of troponin I: influence of PKA phosphorylation and involvement in cardiomyopathies. Baryshnikova OK, Li MX, Sykes BD. J Mol Biol 375 735-751 (2008)
  3. Increasing mammalian cardiomyocyte contractility with residues identified in trout troponin C. Gillis TE, Liang B, Chung F, Tibbits GF. Physiol Genomics 22 1-7 (2005)
  4. Pathogenic peptide deviations support a model of adaptive evolution of chordate cardiac performance by troponin mutations. Palpant NJ, Houang EM, Delport W, Hastings KE, Onufriev AV, Sham YY, Metzger JM. Physiol Genomics 42 287-299 (2010)
  5. Adult teleost heart expresses two distinct troponin C paralogs: cardiac TnC and a novel and teleost-specific ssTnC in a chamber- and temperature-dependent manner. Genge CE, Davidson WS, Tibbits GF. Physiol Genomics 45 866-875 (2013)
  6. Functional characterization of parvalbumin from the Arctic cod (Boreogadus saida): similarity in calcium affinity among parvalbumins from polar teleosts. Erickson JR, Moerland TS. Comp Biochem Physiol A Mol Integr Physiol 143 228-233 (2006)
  7. TnI Structural Interface with the N-Terminal Lobe of TnC as a Determinant of Cardiac Contractility. Vetter AD, Houang EM, Sell JJ, Thompson BR, Sham YY, Metzger JM. Biophys J 114 1646-1656 (2018)
  8. The study of helical distortions due to environmental changes: choice of parameters. Sreekanth R, Rajan SS. Biophys Chem 125 191-200 (2007)
  9. A functional comparison of cardiac troponin C from representatives of three vertebrate taxa: Linking phylogeny and protein function. Sears EJ, Gillis TE. Comp Biochem Physiol B Biochem Mol Biol 202 8-15 (2016)


Related citations provided by authors (1)

  1. Effect of temperature and the F27W mutation on the Ca2+ activated structural transition of trout cardiac troponin C.. Gillis TE, Blumenschein TM, Sykes BD, Tibbits GF Biochemistry 42 6418-26 (2003)

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