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The Myofibrillar Protein, Projectin, is Highly Conserved Across Insect Evolution Except for Its PEVK Domain

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Abstract

All striated muscles respond to stretch by a delayed increase in tension. This physiological response, known as stretch activation, is, however, predominantly found in vertebrate cardiac muscle and insect asynchronous flight muscles. Stretch activation relies on an elastic third filament system composed of giant proteins known as titin in vertebrates or kettin and projectin in insects. The projectin insect protein functions jointly as a “scaffold and ruler” system during myofibril assembly and as an elastic protein during stretch activation. An evolutionary analysis of the projectin molecule could potentially provide insight into how distinct protein regions may have evolved in response to different evolutionary constraints. We mined candidate genes in representative insect species from Hemiptera to Diptera, from published and novel genome sequence data, and carried out a detailed molecular and phylogenetic analysis. The general domain organization of projectin is highly conserved, as are the protein sequences of its two repeated regions—the immunoglobulin type C and fibronectin type III domains. The conservation in structure and sequence is consistent with the proposed function of projectin as a scaffold and ruler. In contrast, the amino acid sequences of the elastic PEVK domains are noticeably divergent, although their length and overall unusual amino acid makeup are conserved. These patterns suggest that the PEVK region working as an unstructured domain can still maintain its dynamic, and even its three-dimensional, properties, without the need for strict amino acid conservation. Phylogenetic analysis of the projectin proteins also supports a reclassification of the Hymenoptera in relation to Diptera and Coleoptera.

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Acknowledgments

This research was supported in part by National Institutes of Health (NIH) Grant 1R15AR053137-01 to AAS. This publication was also made possible by NIH Grant P20 RR-016461 from the National Center for Research Resources. Its contents are solely the responsibility of the authors and do not necessarily represent the official views of the NIH. We thank Dr. J. Evans (USDA, Beltsville, MD), Dr. S. Brown (Kansas State University, Manhattan, KS), Dr. J. Werren (University of Rochester, Rochester, NY), Dr. D. Stern (Princeton University, Princeton, NJ), and the Tucson Drosophila stock center for providing the live insects. We also acknowledge the Human Genome Sequencing Center at Baylor College of Medicine for making accessible the genome sequencing data for Tribolium castaneum, Nasonia vitripennis, and Acyrthosiphon pisum before publication.

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  1. Department of Biology, College of Charleston, 66 George Street, Charleston, SC, 29401, USA

    Agnes J. Ayme-Southgate, Richard J. Southgate, Richard A. Philipp, Erik E. Sotka & Catherine Kramp

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Ayme-Southgate, A.J., Southgate, R.J., Philipp, R.A. et al. The Myofibrillar Protein, Projectin, is Highly Conserved Across Insect Evolution Except for Its PEVK Domain. J Mol Evol 67, 653–669 (2008). https://doi.org/10.1007/s00239-008-9177-2

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