The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression

Abstract Background The structural and biochemical features of the tymbal (sound-producing) muscle of cicadas were studied by X-ray diffraction and immunochemistry, and compared with those of flight muscles from the same species. Results The X-ray diffraction pattern of the tymbal muscle was very si...

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Main Author: Hiroyuki Iwamoto
Format: Article
Language:English
Published: BMC 2017-09-01
Series:Zoological Letters
Subjects:
Online Access:http://link.springer.com/article/10.1186/s40851-017-0077-4
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spelling doaj-fa36a068046e48c5852d371809c222572020-11-25T03:19:00ZengBMCZoological Letters2056-306X2017-09-013111010.1186/s40851-017-0077-4The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expressionHiroyuki Iwamoto0Japan Synchrotron Radiation Research InstituteAbstract Background The structural and biochemical features of the tymbal (sound-producing) muscle of cicadas were studied by X-ray diffraction and immunochemistry, and compared with those of flight muscles from the same species. Results The X-ray diffraction pattern of the tymbal muscle was very similar to that of the dorsal longitudinal flight muscle: In both muscles, the 2,0 equatorial reflection is much more intense than the 1,1, indicating that both muscles have a flight muscle-type myofilament lattice. In rigor, the first myosin/actin layer line reflection was finely lattice-sampled, indicating that the contractile proteins are arranged with a crystalline regularity as in asynchronous flight muscles. In contrast, the diffraction pattern from the tensor muscle, which modulates the sound by stressing the tymbal, did not show signs of such high regularity or flight muscle-type filament lattice. Electrophoretic patterns of myofibrillar proteins were also very similar in the tymbal muscle and flight muscles, but distinct from those from the tensor or leg muscles. The antibody raised against the flight muscle-specific troponin-I isoform reacted with an 80-kDa band from both tymbal and flight muscles, but with none of the bands from the tensor or leg muscles. Conclusion The close similarities of the structural and biochemical profiles between the tymbal and the flight muscles suggest the possibility that a set of flight muscle-specific proteins is diverted to the tymbal muscle to meet its demand for fast, repetitive contractions.http://link.springer.com/article/10.1186/s40851-017-0077-4Tymbal muscleCicadaInsect flight muscleTroponinSynchrotron radiationX-ray diffraction
collection DOAJ
language English
format Article
sources DOAJ
author Hiroyuki Iwamoto
spellingShingle Hiroyuki Iwamoto
The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression
Zoological Letters
Tymbal muscle
Cicada
Insect flight muscle
Troponin
Synchrotron radiation
X-ray diffraction
author_facet Hiroyuki Iwamoto
author_sort Hiroyuki Iwamoto
title The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression
title_short The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression
title_full The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression
title_fullStr The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression
title_full_unstemmed The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression
title_sort tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression
publisher BMC
series Zoological Letters
issn 2056-306X
publishDate 2017-09-01
description Abstract Background The structural and biochemical features of the tymbal (sound-producing) muscle of cicadas were studied by X-ray diffraction and immunochemistry, and compared with those of flight muscles from the same species. Results The X-ray diffraction pattern of the tymbal muscle was very similar to that of the dorsal longitudinal flight muscle: In both muscles, the 2,0 equatorial reflection is much more intense than the 1,1, indicating that both muscles have a flight muscle-type myofilament lattice. In rigor, the first myosin/actin layer line reflection was finely lattice-sampled, indicating that the contractile proteins are arranged with a crystalline regularity as in asynchronous flight muscles. In contrast, the diffraction pattern from the tensor muscle, which modulates the sound by stressing the tymbal, did not show signs of such high regularity or flight muscle-type filament lattice. Electrophoretic patterns of myofibrillar proteins were also very similar in the tymbal muscle and flight muscles, but distinct from those from the tensor or leg muscles. The antibody raised against the flight muscle-specific troponin-I isoform reacted with an 80-kDa band from both tymbal and flight muscles, but with none of the bands from the tensor or leg muscles. Conclusion The close similarities of the structural and biochemical profiles between the tymbal and the flight muscles suggest the possibility that a set of flight muscle-specific proteins is diverted to the tymbal muscle to meet its demand for fast, repetitive contractions.
topic Tymbal muscle
Cicada
Insect flight muscle
Troponin
Synchrotron radiation
X-ray diffraction
url http://link.springer.com/article/10.1186/s40851-017-0077-4
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