Analysis of repetitive amino acid motifs reveals the essential features of spider dragline silk proteins
The extraordinary mechanical properties of spider dragline silk are dependent on the highly repetitive sequences of the component proteins, major ampullate spidroin 1 and 2 (MaSp2 and MaSp2). MaSp sequences are dominated by repetitive modules composed of short amino acid motifs; however, the pattern...
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| creator | Malay, Ali D Arakawa, Kazuharu Numata, Keiji |
| description | The extraordinary mechanical properties of spider dragline silk are dependent on the highly repetitive sequences of the component proteins, major ampullate spidroin 1 and 2 (MaSp2 and MaSp2). MaSp sequences are dominated by repetitive modules composed of short amino acid motifs; however, the patterns of motif conservation through evolution and their relevance to silk characteristics are not well understood. We performed a systematic analysis of MaSp sequences encompassing infraorder Araneomorphae based on the conservation of explicitly defined motifs, with the aim of elucidating the essential elements of MaSp1 and MaSp2. The results show that the GGY motif is nearly ubiquitous in the two types of MaSp, while MaSp2 is invariably associated with GP and di-glutamine (QQ) motifs. Further analysis revealed an extended MaSp2 consensus sequence in family Araneidae, with implications for the classification of the archetypal spidroins ADF3 and ADF4. Additionally, the analysis of RNA-seq data showed the expression of a set of distinct MaSp-like variants in genus Tetragnatha. Finally, an apparent association was uncovered between web architecture and the abundance of GP, QQ, and GGY motifs in MaSp2, which suggests a co-expansion of these motifs in response to the evolution of spiders' prey capture strategy. |
| doi_str_mv | 10.1371/journal.pone.0183397 |
| format | Article |
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MaSp sequences are dominated by repetitive modules composed of short amino acid motifs; however, the patterns of motif conservation through evolution and their relevance to silk characteristics are not well understood. We performed a systematic analysis of MaSp sequences encompassing infraorder Araneomorphae based on the conservation of explicitly defined motifs, with the aim of elucidating the essential elements of MaSp1 and MaSp2. The results show that the GGY motif is nearly ubiquitous in the two types of MaSp, while MaSp2 is invariably associated with GP and di-glutamine (QQ) motifs. Further analysis revealed an extended MaSp2 consensus sequence in family Araneidae, with implications for the classification of the archetypal spidroins ADF3 and ADF4. Additionally, the analysis of RNA-seq data showed the expression of a set of distinct MaSp-like variants in genus Tetragnatha. Finally, an apparent association was uncovered between web architecture and the abundance of GP, QQ, and GGY motifs in MaSp2, which suggests a co-expansion of these motifs in response to the evolution of spiders' prey capture strategy.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0183397</identifier><identifier>PMID: 28832627</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Abundance ; Acids ; Amino Acid Motifs ; Amino Acid Sequence ; Amino acids ; Animals ; Araneidae ; Araneomorphae ; Biology and Life Sciences ; Cellular proteins ; Chemical properties ; Conservation ; Conserved Sequence ; Data processing ; Draglines ; Enzymes ; Evolution ; Evolutionary conservation ; Fibroins - chemistry ; Gene expression ; Genetic research ; Glutamine ; Gluten ; MASP-1 protein ; MASP-2 protein ; Mechanical properties ; Modules ; Physical properties ; Prey ; Proteins ; Research and Analysis Methods ; Ribonucleic acid ; RNA ; Silk ; Silk - chemistry ; Spider silk ; Spiders ; Strength (Materials) ; Studies ; Testing ; Tetragnatha ; Webs</subject><ispartof>PloS one, 2017-08, Vol.12 (8), p.e0183397-e0183397</ispartof><rights>COPYRIGHT 2017 Public Library of Science</rights><rights>2017 Malay et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2017 Malay et al 2017 Malay et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-5923f263e58b30bfa09167f8adbf437f6e327788e46a72b82abdf4aa82d499493</citedby><cites>FETCH-LOGICAL-c758t-5923f263e58b30bfa09167f8adbf437f6e327788e46a72b82abdf4aa82d499493</cites><orcidid>0000-0003-0885-5524</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568437/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568437/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,2103,2929,23871,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28832627$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Zou, Quan</contributor><creatorcontrib>Malay, Ali D</creatorcontrib><creatorcontrib>Arakawa, Kazuharu</creatorcontrib><creatorcontrib>Numata, Keiji</creatorcontrib><title>Analysis of repetitive amino acid motifs reveals the essential features of spider dragline silk proteins</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The extraordinary mechanical properties of spider dragline silk are dependent on the highly repetitive sequences of the component proteins, major ampullate spidroin 1 and 2 (MaSp2 and MaSp2). MaSp sequences are dominated by repetitive modules composed of short amino acid motifs; however, the patterns of motif conservation through evolution and their relevance to silk characteristics are not well understood. We performed a systematic analysis of MaSp sequences encompassing infraorder Araneomorphae based on the conservation of explicitly defined motifs, with the aim of elucidating the essential elements of MaSp1 and MaSp2. The results show that the GGY motif is nearly ubiquitous in the two types of MaSp, while MaSp2 is invariably associated with GP and di-glutamine (QQ) motifs. Further analysis revealed an extended MaSp2 consensus sequence in family Araneidae, with implications for the classification of the archetypal spidroins ADF3 and ADF4. Additionally, the analysis of RNA-seq data showed the expression of a set of distinct MaSp-like variants in genus Tetragnatha. Finally, an apparent association was uncovered between web architecture and the abundance of GP, QQ, and GGY motifs in MaSp2, which suggests a co-expansion of these motifs in response to the evolution of spiders' prey capture strategy.</description><subject>Abundance</subject><subject>Acids</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Araneidae</subject><subject>Araneomorphae</subject><subject>Biology and Life Sciences</subject><subject>Cellular proteins</subject><subject>Chemical properties</subject><subject>Conservation</subject><subject>Conserved Sequence</subject><subject>Data processing</subject><subject>Draglines</subject><subject>Enzymes</subject><subject>Evolution</subject><subject>Evolutionary conservation</subject><subject>Fibroins - chemistry</subject><subject>Gene expression</subject><subject>Genetic research</subject><subject>Glutamine</subject><subject>Gluten</subject><subject>MASP-1 protein</subject><subject>MASP-2 protein</subject><subject>Mechanical properties</subject><subject>Modules</subject><subject>Physical properties</subject><subject>Prey</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Silk</subject><subject>Silk - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Malay, Ali D</au><au>Arakawa, Kazuharu</au><au>Numata, Keiji</au><au>Zou, Quan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of repetitive amino acid motifs reveals the essential features of spider dragline silk proteins</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2017-08-23</date><risdate>2017</risdate><volume>12</volume><issue>8</issue><spage>e0183397</spage><epage>e0183397</epage><pages>e0183397-e0183397</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The extraordinary mechanical properties of spider dragline silk are dependent on the highly repetitive sequences of the component proteins, major ampullate spidroin 1 and 2 (MaSp2 and MaSp2). MaSp sequences are dominated by repetitive modules composed of short amino acid motifs; however, the patterns of motif conservation through evolution and their relevance to silk characteristics are not well understood. We performed a systematic analysis of MaSp sequences encompassing infraorder Araneomorphae based on the conservation of explicitly defined motifs, with the aim of elucidating the essential elements of MaSp1 and MaSp2. The results show that the GGY motif is nearly ubiquitous in the two types of MaSp, while MaSp2 is invariably associated with GP and di-glutamine (QQ) motifs. Further analysis revealed an extended MaSp2 consensus sequence in family Araneidae, with implications for the classification of the archetypal spidroins ADF3 and ADF4. Additionally, the analysis of RNA-seq data showed the expression of a set of distinct MaSp-like variants in genus Tetragnatha. Finally, an apparent association was uncovered between web architecture and the abundance of GP, QQ, and GGY motifs in MaSp2, which suggests a co-expansion of these motifs in response to the evolution of spiders' prey capture strategy.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>28832627</pmid><doi>10.1371/journal.pone.0183397</doi><tpages>e0183397</tpages><orcidid>https://orcid.org/0000-0003-0885-5524</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Abundance Acids Amino Acid Motifs Amino Acid Sequence Amino acids Animals Araneidae Araneomorphae Biology and Life Sciences Cellular proteins Chemical properties Conservation Conserved Sequence Data processing Draglines Enzymes Evolution Evolutionary conservation Fibroins - chemistry Gene expression Genetic research Glutamine Gluten MASP-1 protein MASP-2 protein Mechanical properties Modules Physical properties Prey Proteins Research and Analysis Methods Ribonucleic acid RNA Silk Silk - chemistry Spider silk Spiders Strength (Materials) Studies Testing Tetragnatha Webs |
| title | Analysis of repetitive amino acid motifs reveals the essential features of spider dragline silk proteins |
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