Short inverse complementary amino acid sequences generate protein complexity
Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among proteins registered in SwissProt. The observed number of princoms occurrences excee...
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| Veröffentlicht in: | Comptes rendus. Biologies 2003-03, Vol.326 (3), p.339-348 |
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| container_title | Comptes rendus. Biologies |
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| creator | Goldstein, Daniel J. Fondrat, Christian Muri, Florence Nuel, Gregory Saragueta, Patricia Tocquet, Anne-Sophie Prum, Bernard |
| description | Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among proteins registered in SwissProt. The observed number of princoms occurrences exceeds by far the expected number (
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| doi_str_mv | 10.1016/S1631-0691(03)00077-5 |
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p<10
−10). Princoms often endow their host proteins with a whole new range of biochemical and physiological capabilities, including the possibility of intramolecular and intermolecular disulfide bond formation. These results support the idea that, like the duplications, the inversions of small genomic fragments have been a fundamental mechanism for shaping genomes.
To cite this article: D.J. Goldstein et al., C. R. Biologies 326 (2003).
Le retournement de courtes séquences génomiques joue un rôle central dans la génération de la complexité des protéines. Plus de la moitié des inverses complémentaires des 1300 motifs de ProSite se retrouvent dans les protéines de SwissProt. Le nombre d'occurrences dépasse fortement le nombre attendu (
p<10
−10). Ces résultats renforcent l'idée que, comme les duplications, les inversions de courts segments génomiques ont été un mécanisme fondamental dans l'élaboration des protéines.
Pour citer cet article : D.J. Goldstein et al., C. R. Biologies 326 (2003).</description><identifier>ISSN: 1631-0691</identifier><identifier>ISSN: 1768-3238</identifier><identifier>EISSN: 1768-3238</identifier><identifier>DOI: 10.1016/S1631-0691(03)00077-5</identifier><identifier>PMID: 12806841</identifier><language>eng</language><publisher>Paris: Elsevier SAS</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Apoptosis ; Base Sequence ; Biological and medical sciences ; complexité génomique ; complémentarité inverse ; Databases, Protein ; Disulfides - chemistry ; DNA - chemistry ; Evolution, Molecular ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Genes ; genomic complexity ; genomic inversions ; Hemoglobins - chemistry ; Humans ; Immunoglobulin G - chemistry ; inverse complementary ; inversions génomiques ; Mathematics ; Molecular and cellular biology ; Molecular genetics ; Protein Structure, Tertiary ; Proteins - chemistry ; Proteins - genetics ; von Willebrand Factor - chemistry</subject><ispartof>Comptes rendus. Biologies, 2003-03, Vol.326 (3), p.339-348</ispartof><rights>2003 Académie des sciences/Éditions scientifiques et médicales Elsevier SAS</rights><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c370t-e3664236a4987212d2eefdb75f76ca409e038f51d45cace8d701f63d1cb5ac3a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S1631-0691(03)00077-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14752354$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12806841$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goldstein, Daniel J.</creatorcontrib><creatorcontrib>Fondrat, Christian</creatorcontrib><creatorcontrib>Muri, Florence</creatorcontrib><creatorcontrib>Nuel, Gregory</creatorcontrib><creatorcontrib>Saragueta, Patricia</creatorcontrib><creatorcontrib>Tocquet, Anne-Sophie</creatorcontrib><creatorcontrib>Prum, Bernard</creatorcontrib><title>Short inverse complementary amino acid sequences generate protein complexity</title><title>Comptes rendus. Biologies</title><addtitle>C R Biol</addtitle><description>Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among proteins registered in SwissProt. The observed number of princoms occurrences exceeds by far the expected number (
p<10
−10). Princoms often endow their host proteins with a whole new range of biochemical and physiological capabilities, including the possibility of intramolecular and intermolecular disulfide bond formation. These results support the idea that, like the duplications, the inversions of small genomic fragments have been a fundamental mechanism for shaping genomes.
To cite this article: D.J. Goldstein et al., C. R. Biologies 326 (2003).
Le retournement de courtes séquences génomiques joue un rôle central dans la génération de la complexité des protéines. Plus de la moitié des inverses complémentaires des 1300 motifs de ProSite se retrouvent dans les protéines de SwissProt. Le nombre d'occurrences dépasse fortement le nombre attendu (
p<10
−10). Ces résultats renforcent l'idée que, comme les duplications, les inversions de courts segments génomiques ont été un mécanisme fondamental dans l'élaboration des protéines.
Pour citer cet article : D.J. Goldstein et al., C. R. Biologies 326 (2003).</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>complexité génomique</subject><subject>complémentarité inverse</subject><subject>Databases, Protein</subject><subject>Disulfides - chemistry</subject><subject>DNA - chemistry</subject><subject>Evolution, Molecular</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Genes</subject><subject>genomic complexity</subject><subject>genomic inversions</subject><subject>Hemoglobins - chemistry</subject><subject>Humans</subject><subject>Immunoglobulin G - chemistry</subject><subject>inverse complementary</subject><subject>inversions génomiques</subject><subject>Mathematics</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>von Willebrand Factor - chemistry</subject><issn>1631-0691</issn><issn>1768-3238</issn><issn>1768-3238</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkLtOxDAQRS0E4v0JoDQgKAK2J7aTCiHES1qJYqG2vPYEjPJY7CyCv8e7G0RJNVOcO3N1CDli9IJRJi-nTALLqazYGYVzSqlSudggu0zJMgcO5Wbaf5EdshfjO025SohtssN4SWVZsF0ymb71Ych894khYmb7dt5gi91gwndmWt_1mbHeZRE_FthZjNkrdhjMgNk89AP6bsx8-eH7gGzVpol4OM598nJ3-3zzkE-e7h9vrie5BUWHHEHKgoM0RVUqzrjjiLWbKVEraU1BK6RQ1oK5QlhjsXSKslqCY3YmjAUD--R0fTdVSLXioFsfLTaN6bBfRK0ASl5V6l8QuBS8AkigWIM29DEGrPU8-DY50IzqpW-98q2XMjUFvfKtRcodjw8WsxbdX2oUnICTETDRmqYOprM-_nGFEhxEkbirNYfJ26fHoKP1S-HOB7SDdr3_p8oPU6mdTA</recordid><startdate>20030301</startdate><enddate>20030301</enddate><creator>Goldstein, Daniel J.</creator><creator>Fondrat, Christian</creator><creator>Muri, Florence</creator><creator>Nuel, Gregory</creator><creator>Saragueta, Patricia</creator><creator>Tocquet, Anne-Sophie</creator><creator>Prum, Bernard</creator><general>Elsevier SAS</general><general>Elsevier</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>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20030301</creationdate><title>Short inverse complementary amino acid sequences generate protein complexity</title><author>Goldstein, Daniel J. ; Fondrat, Christian ; Muri, Florence ; Nuel, Gregory ; Saragueta, Patricia ; Tocquet, Anne-Sophie ; Prum, Bernard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c370t-e3664236a4987212d2eefdb75f76ca409e038f51d45cace8d701f63d1cb5ac3a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>complexité génomique</topic><topic>complémentarité inverse</topic><topic>Databases, Protein</topic><topic>Disulfides - chemistry</topic><topic>DNA - chemistry</topic><topic>Evolution, Molecular</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Genes</topic><topic>genomic complexity</topic><topic>genomic inversions</topic><topic>Hemoglobins - chemistry</topic><topic>Humans</topic><topic>Immunoglobulin G - chemistry</topic><topic>inverse complementary</topic><topic>inversions génomiques</topic><topic>Mathematics</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>von Willebrand Factor - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goldstein, Daniel J.</creatorcontrib><creatorcontrib>Fondrat, Christian</creatorcontrib><creatorcontrib>Muri, Florence</creatorcontrib><creatorcontrib>Nuel, Gregory</creatorcontrib><creatorcontrib>Saragueta, Patricia</creatorcontrib><creatorcontrib>Tocquet, Anne-Sophie</creatorcontrib><creatorcontrib>Prum, Bernard</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>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Comptes rendus. Biologies</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goldstein, Daniel J.</au><au>Fondrat, Christian</au><au>Muri, Florence</au><au>Nuel, Gregory</au><au>Saragueta, Patricia</au><au>Tocquet, Anne-Sophie</au><au>Prum, Bernard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Short inverse complementary amino acid sequences generate protein complexity</atitle><jtitle>Comptes rendus. Biologies</jtitle><addtitle>C R Biol</addtitle><date>2003-03-01</date><risdate>2003</risdate><volume>326</volume><issue>3</issue><spage>339</spage><epage>348</epage><pages>339-348</pages><issn>1631-0691</issn><issn>1768-3238</issn><eissn>1768-3238</eissn><abstract>Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among proteins registered in SwissProt. The observed number of princoms occurrences exceeds by far the expected number (
p<10
−10). Princoms often endow their host proteins with a whole new range of biochemical and physiological capabilities, including the possibility of intramolecular and intermolecular disulfide bond formation. These results support the idea that, like the duplications, the inversions of small genomic fragments have been a fundamental mechanism for shaping genomes.
To cite this article: D.J. Goldstein et al., C. R. Biologies 326 (2003).
Le retournement de courtes séquences génomiques joue un rôle central dans la génération de la complexité des protéines. Plus de la moitié des inverses complémentaires des 1300 motifs de ProSite se retrouvent dans les protéines de SwissProt. Le nombre d'occurrences dépasse fortement le nombre attendu (
p<10
−10). Ces résultats renforcent l'idée que, comme les duplications, les inversions de courts segments génomiques ont été un mécanisme fondamental dans l'élaboration des protéines.
Pour citer cet article : D.J. Goldstein et al., C. R. Biologies 326 (2003).</abstract><cop>Paris</cop><pub>Elsevier SAS</pub><pmid>12806841</pmid><doi>10.1016/S1631-0691(03)00077-5</doi><tpages>10</tpages></addata></record> |
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| subjects | Amino Acid Motifs Amino Acid Sequence Animals Apoptosis Base Sequence Biological and medical sciences complexité génomique complémentarité inverse Databases, Protein Disulfides - chemistry DNA - chemistry Evolution, Molecular Fundamental and applied biological sciences. Psychology Gene expression Genes genomic complexity genomic inversions Hemoglobins - chemistry Humans Immunoglobulin G - chemistry inverse complementary inversions génomiques Mathematics Molecular and cellular biology Molecular genetics Protein Structure, Tertiary Proteins - chemistry Proteins - genetics von Willebrand Factor - chemistry |
| title | Short inverse complementary amino acid sequences generate protein complexity |
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