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      https://www.ias.ac.in/article/fulltext/jgen/093/02/0379-0388

    • Keywords

       

      troponin; isoforms; myofibril; flight muscle; Drosophila.

    • Abstract

       

      Troponin proteins in cooperative interaction with tropomyosin are responsible for controlling the contraction of the striated muscles in response to changes in the intracellular calcium concentration. Contractility of the muscle is determined by the constituent protein isoforms, and the isoforms can switch over from one form to another depending on physiological demands and pathological conditions. In Drosophila, amajority of themyofibrillar proteins in the indirect flight muscles (IFMs) undergo post-transcriptional and post-translational isoform changes during pupal to adult metamorphosis to meet the high energy and mechanical demands of flight. Using a newly generated Gal4 strain (UH3-Gal4) which is expressed exclusively in the IFMs, during later stages of development, we have looked at the developmental and functional importance of each of the troponin subunits (troponin-I, troponin-T and troponin-C) and their isoforms. We show that all the troponin subunits are required for normal myofibril assembly and flight, except for the troponin-C isoform 1 (TnC1). Moreover, rescue experiments conducted with troponin-I embryonic isoform in the IFMs, where flies were rendered flightless, show developmental and functional differences of TnI isoforms and importance of maintaining the right isoform.

    • Author Affiliations

       

      Salam Herojeet Singh1 2 Prabodh Kumar1 Nallur B. Ramachandra2 Upendra Nongthomba1

      1. Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560 012, India
      2. Department of Studies in Zoology, University of Mysore, Manasagangotri, Mysore 570 006, India
    • Dates

       
  • Journal of Genetics | News

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