Cuticular protein with a low complexity sequence becomes cross-linked during insect cuticle sclerotization and is required for the adult molt

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dc.contributor.author Mun, S.
dc.contributor.author Noh, M. Y.
dc.contributor.author Dittmer, Neal Thomas
dc.contributor.author Muthukrishnan, Subbaratnam
dc.contributor.author Kramer, K. J.
dc.contributor.author Kanost, Michael R.
dc.contributor.author Arakane, Yasuyuki
dc.date.accessioned 2016-03-28T19:20:15Z
dc.date.available 2016-03-28T19:20:15Z
dc.date.issued 2015-05-21
dc.identifier.uri http://hdl.handle.net/2097/32199
dc.description Citation: Mun, S., Noh, M. Y., Dittmer, N. T., Muthukrishnan, S., Kramer, K. J., Kanost, M. R., & Arakane, Y. (2015). Cuticular protein with a low complexity sequence becomes cross-linked during insect cuticle sclerotization and is required for the adult molt. Scientific Reports, 5, 11. doi:10.1038/srep10484
dc.description In the insect cuticle, structural proteins (CPs) and the polysaccharide chitin are the major components. It has been hypothesized that CPs are cross-linked to other CPs and possibly to chitin by quinones or quinone methides produced by the laccase2-mediated oxidation of N-acylcatechols. In this study we investigated functions of TcCP30, the third most abundant CP in protein extracts of elytra (wing covers) from Tribolium castaneum adults. The mature TcCP30 protein has a low complexity and highly polar amino acid sequence. TcCP30 is localized with chitin in horizontal laminae and vertically oriented columnar structures in rigid cuticles, but not in soft and membranous cuticles. Immunoblot analysis revealed that TcCP30 undergoes laccase2-mediated cross-linking during cuticle maturation in vivo, a process confirmed in vitro using recombinant rTcCP30. We identified TcCPR27 and TcCPR18, the two most abundant proteins in the elytra, as putative crosslinking partners of TcCP30. RNAi for the TcCP30 gene had no effect on larval and pupal growth and development. However, during adult eclosion, similar to 70% of the adults were unable to shed their exuvium and died. These results support the hypothesis that TcCP30 plays an integral role as a cross-linked structural protein in the formation of lightweight rigid cuticle of the beetle.
dc.relation.uri https://doi.org/10.1038/srep10484
dc.rights Attribution 4.0 International (CC BY 4.0)
dc.rights.uri http://creativecommons.org/licenses/by/4.0/
dc.subject Tribolium-Castaneum
dc.subject Anopheles-Gambiae
dc.subject Bombyx-Mori
dc.subject R Consensus
dc.subject Genes
dc.subject Expression
dc.title Cuticular protein with a low complexity sequence becomes cross-linked during insect cuticle sclerotization and is required for the adult molt
dc.type Article
dc.date.published 2015
dc.citation.doi 10.1038/srep10484
dc.citation.issn 2045-2322
dc.citation.jtitle Scientific Reports
dc.citation.spage 11
dc.citation.volume 5
dc.contributor.authoreid ndittmer
dc.contributor.authoreid smk
dc.contributor.authoreid kanost


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