Journal
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume 43, Issue 12, Pages 1181-1188Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.ibmb.2013.09.008
Keywords
Black fly; Simulium vittatum; Silk proteins; Silk genes; Phosphoproteins; Transcriptomics; Proteomics
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Funding
- Creighton University College of Arts and Science
- Creighton University Division of Academic Affairs
- Office of the Chief Executive (OCE) of the Commonwealth Scientific and Industrial Research Organisation (CSIRO)
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The silks of arthropods have an elementary role in the natural history of the organisms that spin them, yet they are coded by rapidly evolving genes leading some authors to speculate that silk proteins are non-homologous proteins co-opted multiple times independently for similar functions. However, some general structural patterns are emerging. In this work we identified three major silk gland proteins using a combined biochemical, proteomic, next-generation sequencing and bioinformatic approach. Biochemical characterization determined that they were phosphorylated with multiple isoforms and potentially differential phosphorylation. Structural characterization showed that their structure was more similar to silk proteins from distantly related aquatic Trichopteran species than more closely related terrestrial or aquatic Diptera. Overall, our approach is easily transferable to any non-model species and if used across a larger number of aquatic species, we will be able to better understand the processes involved in linking the secondary structure of silk proteins with their function between in an organisms and its habitat. (C) 2013 Elsevier Ltd. All rights reserved.
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