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Biology 2016, 5(2), 16; doi:10.3390/biology5020016

The Contributions of the Amino and Carboxy Terminal Domains of Flightin to the Biomechanical Properties of Drosophila Flight Muscle Thick Filaments

1
Department of Biology, University of Vermont, Burlington, VT 05405, USA
2
Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA
*
Author to whom correspondence should be addressed.
Academic Editors: Chris O’Callaghan and Jukka Finne
Received: 17 March 2016 / Revised: 15 April 2016 / Accepted: 18 April 2016 / Published: 27 April 2016
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Abstract

Flightin is a myosin binding protein present in Pancrustacea. In Drosophila, flightin is expressed in the indirect flight muscles (IFM), where it is required for the flexural rigidity, structural integrity, and length determination of thick filaments. Comparison of flightin sequences from multiple Drosophila species revealed a tripartite organization indicative of three functional domains subject to different evolutionary constraints. We use atomic force microscopy to investigate the functional roles of the N-terminal domain and the C-terminal domain that show different patterns of sequence conservation. Thick filaments containing a C-terminal domain truncated flightin (flnΔC44) are significantly shorter (2.68 ± 0.06 μm; p < 0.005) than thick filaments containing a full length flightin (fln+; 3.21 ± 0.05 μm) and thick filaments containing an N-terminal domain truncated flightin (flnΔN62; 3.21 ± 0.06 μm). Persistence length was significantly reduced in flnΔN62 (418 ± 72 μm; p < 0.005) compared to fln+ (1386 ± 196μm) and flnΔC44(1128 ± 193 μm). Statistical polymer chain analysis revealed that the C-terminal domain fulfills a secondary role in thick filament bending propensity. Our results indicate that the flightin amino and carboxy terminal domains make distinct contributions to thick filament biomechanics. We propose these distinct roles arise from the interplay between natural selection and sexual selection given IFM’s dual role in flight and courtship behaviors. View Full-Text
Keywords: flightin; Drosophila melanogaster; myosin; thick filament; persistence length; atomic force microscopy flightin; Drosophila melanogaster; myosin; thick filament; persistence length; atomic force microscopy
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Gasek, N.S.; Nyland, L.R.; Vigoreaux, J.O. The Contributions of the Amino and Carboxy Terminal Domains of Flightin to the Biomechanical Properties of Drosophila Flight Muscle Thick Filaments. Biology 2016, 5, 16.

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