Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1181-1188 |
| Number of pages | 8 |
| Journal | Insect Biochemistry and Molecular Biology |
| Volume | 43 |
| Issue number | 12 |
| DOIs | |
| State | Published - Dec 2013 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Insect Science
Cite this
Novel aquatic silk genes from Simulium (Psilozia) vittatum (Zett) Diptera : Simuliidae. / Papanicolaou, Alexie; Woo, Angelica; Brei, Brianna; Ma, Danjun; Masedunskas, Andrius; Gray, Elmer; Xiao, Gary Guishan; Cho, Soochin; Brockhouse, Charles.
In: Insect Biochemistry and Molecular Biology, Vol. 43, No. 12, 12.2013, p. 1181-1188.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Novel aquatic silk genes from Simulium (Psilozia) vittatum (Zett) Diptera
T2 - Simuliidae
AU - Papanicolaou, Alexie
AU - Woo, Angelica
AU - Brei, Brianna
AU - Ma, Danjun
AU - Masedunskas, Andrius
AU - Gray, Elmer
AU - Xiao, Gary Guishan
AU - Cho, Soochin
AU - Brockhouse, Charles
PY - 2013/12
Y1 - 2013/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84887171247&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84887171247&partnerID=8YFLogxK
U2 - 10.1016/j.ibmb.2013.09.008
DO - 10.1016/j.ibmb.2013.09.008
M3 - Article
C2 - 24446544
AN - SCOPUS:84887171247
VL - 43
SP - 1181
EP - 1188
JO - Insect Biochemistry and Molecular Biology
JF - Insect Biochemistry and Molecular Biology
SN - 0965-1748
IS - 12
ER -