Evolution of collagen IV genes from a 54-base pair exon : a role for introns in gene evolution
The exon structure of the collagen IV gene provides a striking example for collagen evolution and the role of introns in gene evolution. Collagen IV, a major component of basement membranes, differs from the fibrillar collagens in that it contains numerous interruptions in the triple helical Gly-X-Y...
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Veröffentlicht in: | Journal of molecular evolution 1990-06, Vol.30 (6), p.479-488 |
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description | The exon structure of the collagen IV gene provides a striking example for collagen evolution and the role of introns in gene evolution. Collagen IV, a major component of basement membranes, differs from the fibrillar collagens in that it contains numerous interruptions in the triple helical Gly-X-Y repeat domain. We have characterized all 47 exons in the mouse alpha 2(IV) collagen gene and find two 36-, two 45-, and one 54-bp exons as well as one 99- and three 108-bp exons encoding the Gly-X-Y repeat sequence. All these exons sizes are also found in the fibrillar collagen genes. Strikingly, of the 24 interruption sequences present in the alpha 2-chain of mouse collagen IV, 11 are encoded at the exon/intron borders of the gene, part of one interruption sequence is encoded by an exon of its own, and the remaining interruptions are encoded within the body of exons. In such "fusion exons" the Gly-X-Y encoding domain is also derived from 36-, 45-, or 54-bp sequence elements. These data support the idea that collagen IV genes evolved from a primordial 54-bp coding unit. We furthermore interpret these data to suggest that the interruption sequences in collagen IV may have evolved from introns, presumably by inactivation of splice site signals, following which intronic sequences could have been recruited into exons. We speculated that this mechanism could provide a role for introns in gene evolution in general. |
doi_str_mv | 10.1007/BF02101102 |
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Collagen IV, a major component of basement membranes, differs from the fibrillar collagens in that it contains numerous interruptions in the triple helical Gly-X-Y repeat domain. We have characterized all 47 exons in the mouse alpha 2(IV) collagen gene and find two 36-, two 45-, and one 54-bp exons as well as one 99- and three 108-bp exons encoding the Gly-X-Y repeat sequence. All these exons sizes are also found in the fibrillar collagen genes. Strikingly, of the 24 interruption sequences present in the alpha 2-chain of mouse collagen IV, 11 are encoded at the exon/intron borders of the gene, part of one interruption sequence is encoded by an exon of its own, and the remaining interruptions are encoded within the body of exons. In such "fusion exons" the Gly-X-Y encoding domain is also derived from 36-, 45-, or 54-bp sequence elements. These data support the idea that collagen IV genes evolved from a primordial 54-bp coding unit. We furthermore interpret these data to suggest that the interruption sequences in collagen IV may have evolved from introns, presumably by inactivation of splice site signals, following which intronic sequences could have been recruited into exons. We speculated that this mechanism could provide a role for introns in gene evolution in general.</description><identifier>ISSN: 0022-2844</identifier><identifier>EISSN: 1432-1432</identifier><identifier>DOI: 10.1007/BF02101102</identifier><identifier>PMID: 2115927</identifier><identifier>CODEN: JMEVAU</identifier><language>eng</language><publisher>New York, NY: Springer</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Biological Evolution ; Collagen - genetics ; Exons ; Fundamental and applied biological sciences. Psychology ; Genes ; Genetics of eukaryotes. 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Collagen IV, a major component of basement membranes, differs from the fibrillar collagens in that it contains numerous interruptions in the triple helical Gly-X-Y repeat domain. We have characterized all 47 exons in the mouse alpha 2(IV) collagen gene and find two 36-, two 45-, and one 54-bp exons as well as one 99- and three 108-bp exons encoding the Gly-X-Y repeat sequence. All these exons sizes are also found in the fibrillar collagen genes. Strikingly, of the 24 interruption sequences present in the alpha 2-chain of mouse collagen IV, 11 are encoded at the exon/intron borders of the gene, part of one interruption sequence is encoded by an exon of its own, and the remaining interruptions are encoded within the body of exons. In such "fusion exons" the Gly-X-Y encoding domain is also derived from 36-, 45-, or 54-bp sequence elements. These data support the idea that collagen IV genes evolved from a primordial 54-bp coding unit. We furthermore interpret these data to suggest that the interruption sequences in collagen IV may have evolved from introns, presumably by inactivation of splice site signals, following which intronic sequences could have been recruited into exons. We speculated that this mechanism could provide a role for introns in gene evolution in general.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biological Evolution</subject><subject>Collagen - genetics</subject><subject>Exons</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Genetics of eukaryotes. Biological and molecular evolution</subject><subject>Introns</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Repetitive Sequences, Nucleic Acid</subject><subject>RNA Splicing</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Space life sciences</subject><issn>0022-2844</issn><issn>1432-1432</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM1LAzEQxYMotVYv3oVc9CCs5rPZeNPSaqHgRT26ZLMTWdnd1KQV_e9N7WoPMw9mfvNgHkKnlFxRQtT13YwwSiglbA8NqeAs27R9NCSEsYzlQhyioxjfCaFKaj5AA0ap1EwN0ev00zfrVe077B22vmnMG3R4_oKTQMQu-BYbLEVWmgh4aeqA4SvRN2kafAPY-YDrbhV8F5P-nmH4Mz1GB840EU56HaHn2fRp8pAtHu_nk9tFZjllqwxUXlErhdKlcJLRVGPjdOm4gMoxpiiMqZCq4pKDVeBIrvKyIpLYPDdjzUfoYuu7DP5jDXFVtHW0kL7pwK9jobQmkguSwMstaIOPMYArlqFuTfguKCk2YRa7MBN81ruuyxaqf7RPL-3P-72J1jQumM7WceeouZY05_wHUFZ5qA</recordid><startdate>199006</startdate><enddate>199006</enddate><creator>BUTTICE, G</creator><creator>KAYTES, P</creator><creator>D'ARMIENTO, J</creator><creator>VOGELI, G</creator><creator>KURKINEN, M</creator><general>Springer</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199006</creationdate><title>Evolution of collagen IV genes from a 54-base pair exon : a role for introns in gene evolution</title><author>BUTTICE, G ; KAYTES, P ; D'ARMIENTO, J ; VOGELI, G ; KURKINEN, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c312t-e78d1c5479b4f521f526af9bf34edf2271e61457d353ec7ef0878bd050c88a693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biological Evolution</topic><topic>Collagen - genetics</topic><topic>Exons</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes</topic><topic>Genetics of eukaryotes. Biological and molecular evolution</topic><topic>Introns</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Repetitive Sequences, Nucleic Acid</topic><topic>RNA Splicing</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Space life sciences</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BUTTICE, G</creatorcontrib><creatorcontrib>KAYTES, P</creatorcontrib><creatorcontrib>D'ARMIENTO, J</creatorcontrib><creatorcontrib>VOGELI, G</creatorcontrib><creatorcontrib>KURKINEN, M</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular evolution</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BUTTICE, G</au><au>KAYTES, P</au><au>D'ARMIENTO, J</au><au>VOGELI, G</au><au>KURKINEN, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evolution of collagen IV genes from a 54-base pair exon : a role for introns in gene evolution</atitle><jtitle>Journal of molecular evolution</jtitle><addtitle>J Mol Evol</addtitle><date>1990-06</date><risdate>1990</risdate><volume>30</volume><issue>6</issue><spage>479</spage><epage>488</epage><pages>479-488</pages><issn>0022-2844</issn><eissn>1432-1432</eissn><coden>JMEVAU</coden><abstract>The exon structure of the collagen IV gene provides a striking example for collagen evolution and the role of introns in gene evolution. Collagen IV, a major component of basement membranes, differs from the fibrillar collagens in that it contains numerous interruptions in the triple helical Gly-X-Y repeat domain. We have characterized all 47 exons in the mouse alpha 2(IV) collagen gene and find two 36-, two 45-, and one 54-bp exons as well as one 99- and three 108-bp exons encoding the Gly-X-Y repeat sequence. All these exons sizes are also found in the fibrillar collagen genes. Strikingly, of the 24 interruption sequences present in the alpha 2-chain of mouse collagen IV, 11 are encoded at the exon/intron borders of the gene, part of one interruption sequence is encoded by an exon of its own, and the remaining interruptions are encoded within the body of exons. In such "fusion exons" the Gly-X-Y encoding domain is also derived from 36-, 45-, or 54-bp sequence elements. These data support the idea that collagen IV genes evolved from a primordial 54-bp coding unit. We furthermore interpret these data to suggest that the interruption sequences in collagen IV may have evolved from introns, presumably by inactivation of splice site signals, following which intronic sequences could have been recruited into exons. We speculated that this mechanism could provide a role for introns in gene evolution in general.</abstract><cop>New York, NY</cop><pub>Springer</pub><pmid>2115927</pmid><doi>10.1007/BF02101102</doi><tpages>10</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Biological Evolution Collagen - genetics Exons Fundamental and applied biological sciences. Psychology Genes Genetics of eukaryotes. Biological and molecular evolution Introns Mice Molecular Sequence Data Repetitive Sequences, Nucleic Acid RNA Splicing Sequence Homology, Nucleic Acid Space life sciences |
title | Evolution of collagen IV genes from a 54-base pair exon : a role for introns in gene evolution |
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