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CPAP3 proteins in the mineralized cuticle of a decapod crustacean
The pancrustacean theory groups crustaceans and hexapods (once thought to comprise separate clades within the Arthropoda) into a single clade. A key feature common to all pancrustaceans is their chitinous exoskeleton, with a major contribution by cuticular proteins. Among these, are the CPAP3’s, a f...
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Published in: | Scientific reports 2018-02, Vol.8 (1), p.2430-12, Article 2430 |
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creator | Abehsera, Shai Zaccai, Shir Mittelman, Binyamin Glazer, Lilah Weil, Simy Khalaila, Isam Davidov, Geula Bitton, Ronit Zarivach, Raz Li, Shihao Li, Fuhua Xiang, Jianhai Manor, Rivka Aflalo, Eliahu D. Sagi, Amir |
description | The pancrustacean theory groups crustaceans and hexapods (once thought to comprise separate clades within the Arthropoda) into a single clade. A key feature common to all pancrustaceans is their chitinous exoskeleton, with a major contribution by cuticular proteins. Among these, are the CPAP3’s, a family of cuticular proteins, first identified in the hexapod
Drosophila melanogaster
and characterized by an N-terminal signaling peptide and three chitin-binding domains. In this study, CPAP3 proteins were mined from a transcriptomic library of a decapod crustacean, the crayfish
Cherax quadricarinatus
. Phylogenetic analysis of other CPAP3 proteins from hexapods and other crustaceans showed a high degree of conservation. Characterization of the crayfish proteins, designated CqCPAP3’s, suggested a major role for CPAP3’sin cuticle formation. Loss-of-function experiments using RNAi supported such a notion by demonstrating crucial roles for several CqCPAP3 proteins during molting. A putative mode of action for the CqCPAP3 proteins –theoretically binding three chitin strands– was suggested by the structural data obtained from a representative recombinant CqCPAP3. The similarities between the CqCPAP3 proteins and their hexapod homologues further demonstrated common genetic and proteinaceous features of cuticle formation in pancrustaceans, thereby reinforcing the linkage between these two highly important phylogenetic groups. |
doi_str_mv | 10.1038/s41598-018-20835-x |
format | article |
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Drosophila melanogaster
and characterized by an N-terminal signaling peptide and three chitin-binding domains. In this study, CPAP3 proteins were mined from a transcriptomic library of a decapod crustacean, the crayfish
Cherax quadricarinatus
. Phylogenetic analysis of other CPAP3 proteins from hexapods and other crustaceans showed a high degree of conservation. Characterization of the crayfish proteins, designated CqCPAP3’s, suggested a major role for CPAP3’sin cuticle formation. Loss-of-function experiments using RNAi supported such a notion by demonstrating crucial roles for several CqCPAP3 proteins during molting. A putative mode of action for the CqCPAP3 proteins –theoretically binding three chitin strands– was suggested by the structural data obtained from a representative recombinant CqCPAP3. The similarities between the CqCPAP3 proteins and their hexapod homologues further demonstrated common genetic and proteinaceous features of cuticle formation in pancrustaceans, thereby reinforcing the linkage between these two highly important phylogenetic groups.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-018-20835-x</identifier><identifier>PMID: 29403068</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/28 ; 38 ; 38/23 ; 38/77 ; 38/89 ; 631/181/735 ; 631/337/475 ; 82 ; 82/58 ; 82/80 ; Animal Shells - chemistry ; Animal Shells - metabolism ; Animals ; Arthropod Proteins - antagonists & inhibitors ; Arthropod Proteins - chemistry ; Arthropod Proteins - genetics ; Arthropod Proteins - metabolism ; Astacoidea - classification ; Astacoidea - genetics ; Astacoidea - metabolism ; Biomineralization - genetics ; Chitin ; Chitin - biosynthesis ; Chitin - chemistry ; Chitin - genetics ; Cloning, Molecular ; Crustacea ; Crustaceans ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Exoskeleton ; Gene Expression ; Genetic Vectors - chemistry ; Genetic Vectors - metabolism ; Hexapoda ; Humanities and Social Sciences ; Insecta - classification ; Insecta - genetics ; Insecta - metabolism ; Mode of action ; Molting ; multidisciplinary ; Phylogenetics ; Phylogeny ; Protein Isoforms - antagonists & inhibitors ; Protein Isoforms - chemistry ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; RNA, Small Interfering - genetics ; RNA, Small Interfering - metabolism ; RNA-mediated interference ; Science ; Science (multidisciplinary) ; Transcriptome</subject><ispartof>Scientific reports, 2018-02, Vol.8 (1), p.2430-12, Article 2430</ispartof><rights>The Author(s) 2018</rights><rights>2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c540t-60d2664c1b70a64548a984fc2cde4638bd9e25d9a693326276cad19c4c92c7873</citedby><cites>FETCH-LOGICAL-c540t-60d2664c1b70a64548a984fc2cde4638bd9e25d9a693326276cad19c4c92c7873</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1994396026/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1994396026?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29403068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abehsera, Shai</creatorcontrib><creatorcontrib>Zaccai, Shir</creatorcontrib><creatorcontrib>Mittelman, Binyamin</creatorcontrib><creatorcontrib>Glazer, Lilah</creatorcontrib><creatorcontrib>Weil, Simy</creatorcontrib><creatorcontrib>Khalaila, Isam</creatorcontrib><creatorcontrib>Davidov, Geula</creatorcontrib><creatorcontrib>Bitton, Ronit</creatorcontrib><creatorcontrib>Zarivach, Raz</creatorcontrib><creatorcontrib>Li, Shihao</creatorcontrib><creatorcontrib>Li, Fuhua</creatorcontrib><creatorcontrib>Xiang, Jianhai</creatorcontrib><creatorcontrib>Manor, Rivka</creatorcontrib><creatorcontrib>Aflalo, Eliahu D.</creatorcontrib><creatorcontrib>Sagi, Amir</creatorcontrib><title>CPAP3 proteins in the mineralized cuticle of a decapod crustacean</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>The pancrustacean theory groups crustaceans and hexapods (once thought to comprise separate clades within the Arthropoda) into a single clade. A key feature common to all pancrustaceans is their chitinous exoskeleton, with a major contribution by cuticular proteins. Among these, are the CPAP3’s, a family of cuticular proteins, first identified in the hexapod
Drosophila melanogaster
and characterized by an N-terminal signaling peptide and three chitin-binding domains. In this study, CPAP3 proteins were mined from a transcriptomic library of a decapod crustacean, the crayfish
Cherax quadricarinatus
. Phylogenetic analysis of other CPAP3 proteins from hexapods and other crustaceans showed a high degree of conservation. Characterization of the crayfish proteins, designated CqCPAP3’s, suggested a major role for CPAP3’sin cuticle formation. Loss-of-function experiments using RNAi supported such a notion by demonstrating crucial roles for several CqCPAP3 proteins during molting. A putative mode of action for the CqCPAP3 proteins –theoretically binding three chitin strands– was suggested by the structural data obtained from a representative recombinant CqCPAP3. The similarities between the CqCPAP3 proteins and their hexapod homologues further demonstrated common genetic and proteinaceous features of cuticle formation in pancrustaceans, thereby reinforcing the linkage between these two highly important phylogenetic groups.</description><subject>101/28</subject><subject>38</subject><subject>38/23</subject><subject>38/77</subject><subject>38/89</subject><subject>631/181/735</subject><subject>631/337/475</subject><subject>82</subject><subject>82/58</subject><subject>82/80</subject><subject>Animal Shells - chemistry</subject><subject>Animal Shells - metabolism</subject><subject>Animals</subject><subject>Arthropod Proteins - antagonists & inhibitors</subject><subject>Arthropod Proteins - chemistry</subject><subject>Arthropod Proteins - genetics</subject><subject>Arthropod Proteins - metabolism</subject><subject>Astacoidea - classification</subject><subject>Astacoidea - genetics</subject><subject>Astacoidea - metabolism</subject><subject>Biomineralization - 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A key feature common to all pancrustaceans is their chitinous exoskeleton, with a major contribution by cuticular proteins. Among these, are the CPAP3’s, a family of cuticular proteins, first identified in the hexapod
Drosophila melanogaster
and characterized by an N-terminal signaling peptide and three chitin-binding domains. In this study, CPAP3 proteins were mined from a transcriptomic library of a decapod crustacean, the crayfish
Cherax quadricarinatus
. Phylogenetic analysis of other CPAP3 proteins from hexapods and other crustaceans showed a high degree of conservation. Characterization of the crayfish proteins, designated CqCPAP3’s, suggested a major role for CPAP3’sin cuticle formation. Loss-of-function experiments using RNAi supported such a notion by demonstrating crucial roles for several CqCPAP3 proteins during molting. A putative mode of action for the CqCPAP3 proteins –theoretically binding three chitin strands– was suggested by the structural data obtained from a representative recombinant CqCPAP3. The similarities between the CqCPAP3 proteins and their hexapod homologues further demonstrated common genetic and proteinaceous features of cuticle formation in pancrustaceans, thereby reinforcing the linkage between these two highly important phylogenetic groups.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29403068</pmid><doi>10.1038/s41598-018-20835-x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 101/28 38 38/23 38/77 38/89 631/181/735 631/337/475 82 82/58 82/80 Animal Shells - chemistry Animal Shells - metabolism Animals Arthropod Proteins - antagonists & inhibitors Arthropod Proteins - chemistry Arthropod Proteins - genetics Arthropod Proteins - metabolism Astacoidea - classification Astacoidea - genetics Astacoidea - metabolism Biomineralization - genetics Chitin Chitin - biosynthesis Chitin - chemistry Chitin - genetics Cloning, Molecular Crustacea Crustaceans Escherichia coli - genetics Escherichia coli - metabolism Exoskeleton Gene Expression Genetic Vectors - chemistry Genetic Vectors - metabolism Hexapoda Humanities and Social Sciences Insecta - classification Insecta - genetics Insecta - metabolism Mode of action Molting multidisciplinary Phylogenetics Phylogeny Protein Isoforms - antagonists & inhibitors Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA, Small Interfering - genetics RNA, Small Interfering - metabolism RNA-mediated interference Science Science (multidisciplinary) Transcriptome |
title | CPAP3 proteins in the mineralized cuticle of a decapod crustacean |
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