A tropomyosin-2 mutation suppresses a troponin I myopathy in Drosophila
A suppressor mutation, D53, of the held-up(2) allele of the Drosophila melanogaster Troponin I (wupA) gene is described. D53, a missense mutation, S185F, of the tropomyosin-2, Tm2, gene fully suppresses all the phenotypic effects of held-up(2), including the destructive hypercontraction of the indir...
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Veröffentlicht in: | Molecular biology of the cell 2001-05, Vol.12 (5), p.1529-1539 |
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creator | Naimi, B Harrison, A Cummins, M Nongthomba, U Clark, S Canal, I Ferrus, A Sparrow, J C |
description | A suppressor mutation, D53, of the held-up(2) allele of the Drosophila melanogaster Troponin I (wupA) gene is described. D53, a missense mutation, S185F, of the tropomyosin-2, Tm2, gene fully suppresses all the phenotypic effects of held-up(2), including the destructive hypercontraction of the indirect flight muscles (IFMs), a lack of jumping, the progressive myopathy of the walking muscles, and reductions in larval crawling and feeding behavior. The suppressor restores normal function of the IFMs, but flight ability decreases with age and correlates with an unusual, progressive structural collapse of the myofibrillar lattice starting at the center. The S185F substitution in Tm2 is close to a troponin T binding site on tropomyosin. Models to explain suppression by D53, derived from current knowledge of the vertebrate troponin-tropomyosin complex structure and functions, are discussed. The effects of S185F are compared with those of two mutations in residues 175 and 180 of human alpha-tropomyosin 1 which cause familial hypertrophic cardiomyopathy (HCM). |
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D53, a missense mutation, S185F, of the tropomyosin-2, Tm2, gene fully suppresses all the phenotypic effects of held-up(2), including the destructive hypercontraction of the indirect flight muscles (IFMs), a lack of jumping, the progressive myopathy of the walking muscles, and reductions in larval crawling and feeding behavior. The suppressor restores normal function of the IFMs, but flight ability decreases with age and correlates with an unusual, progressive structural collapse of the myofibrillar lattice starting at the center. The S185F substitution in Tm2 is close to a troponin T binding site on tropomyosin. Models to explain suppression by D53, derived from current knowledge of the vertebrate troponin-tropomyosin complex structure and functions, are discussed. The effects of S185F are compared with those of two mutations in residues 175 and 180 of human alpha-tropomyosin 1 which cause familial hypertrophic cardiomyopathy (HCM).</description><identifier>ISSN: 1059-1524</identifier><identifier>EISSN: 1939-4586</identifier><identifier>DOI: 10.1091/mbc.12.5.1529</identifier><identifier>PMID: 11359941</identifier><language>eng</language><publisher>United States: The American Society for Cell Biology</publisher><subject>Amino Acid Sequence ; Animals ; Behavior, Animal - physiology ; Drosophila melanogaster - genetics ; Drosophila melanogaster - growth & development ; Drosophila melanogaster - physiology ; Flight, Animal - physiology ; Humans ; Larva - physiology ; Male ; Molecular Sequence Data ; Muscle Contraction - physiology ; Muscle, Skeletal - physiology ; Muscle, Skeletal - ultrastructure ; Mutation, Missense - genetics ; Phenotype ; Sequence Alignment ; Suppression, Genetic - genetics ; Tropomyosin - genetics ; Tropomyosin - metabolism ; Troponin I - genetics ; Troponin I - metabolism</subject><ispartof>Molecular biology of the cell, 2001-05, Vol.12 (5), p.1529-1539</ispartof><rights>Copyright © 2001, The American Society for Cell Biology 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c373t-8e4107b984540fa68f1afd0123370afb9a6e83a5dbb90d0e5d0b08dbc5b7ad8d3</citedby><cites>FETCH-LOGICAL-c373t-8e4107b984540fa68f1afd0123370afb9a6e83a5dbb90d0e5d0b08dbc5b7ad8d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC34603/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC34603/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,729,782,786,887,27931,27932,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11359941$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Pringle, John</contributor><creatorcontrib>Naimi, B</creatorcontrib><creatorcontrib>Harrison, A</creatorcontrib><creatorcontrib>Cummins, M</creatorcontrib><creatorcontrib>Nongthomba, U</creatorcontrib><creatorcontrib>Clark, S</creatorcontrib><creatorcontrib>Canal, I</creatorcontrib><creatorcontrib>Ferrus, A</creatorcontrib><creatorcontrib>Sparrow, J C</creatorcontrib><title>A tropomyosin-2 mutation suppresses a troponin I myopathy in Drosophila</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>A suppressor mutation, D53, of the held-up(2) allele of the Drosophila melanogaster Troponin I (wupA) gene is described. D53, a missense mutation, S185F, of the tropomyosin-2, Tm2, gene fully suppresses all the phenotypic effects of held-up(2), including the destructive hypercontraction of the indirect flight muscles (IFMs), a lack of jumping, the progressive myopathy of the walking muscles, and reductions in larval crawling and feeding behavior. The suppressor restores normal function of the IFMs, but flight ability decreases with age and correlates with an unusual, progressive structural collapse of the myofibrillar lattice starting at the center. The S185F substitution in Tm2 is close to a troponin T binding site on tropomyosin. Models to explain suppression by D53, derived from current knowledge of the vertebrate troponin-tropomyosin complex structure and functions, are discussed. The effects of S185F are compared with those of two mutations in residues 175 and 180 of human alpha-tropomyosin 1 which cause familial hypertrophic cardiomyopathy (HCM).</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Behavior, Animal - physiology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila melanogaster - growth & development</subject><subject>Drosophila melanogaster - physiology</subject><subject>Flight, Animal - physiology</subject><subject>Humans</subject><subject>Larva - physiology</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Muscle Contraction - physiology</subject><subject>Muscle, Skeletal - physiology</subject><subject>Muscle, Skeletal - ultrastructure</subject><subject>Mutation, Missense - genetics</subject><subject>Phenotype</subject><subject>Sequence Alignment</subject><subject>Suppression, Genetic - genetics</subject><subject>Tropomyosin - genetics</subject><subject>Tropomyosin - metabolism</subject><subject>Troponin I - genetics</subject><subject>Troponin I - metabolism</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkLtOwzAUhi0EoqUwsqJMbCnHsZ3YEktVoFSqxAKzZccONUriECdIfXtcteIyndt3bj9C1xjmGAS-a3Q5x9mczTHLxAmaYkFEShnPT6MPTKQxTyfoIoQPAExpXpyjCcaECUHxFK0WydD7zjc7H1ybZkkzDmpwvk3C2HW9DcGGRB2Y1rXJOolkp4btLonRQ--D77auVpforFJ1sFdHO0NvT4-vy-d087JaLxebtCQFGVJuKYZCC04ZhUrlvMKqMoAzQgpQlRYqt5woZrQWYMAyAxq40SXThTLckBm6P8ztRt1YU9p26FUtu941qt9Jr5z8X2ndVr77L0loDiS23x7be_852jDIxoXS1rVqrR-DLIDnGRcQwfQAlvHF0NvqZwUGuRdeRuElziSTe-Ejf_P3rl_6qDT5BunRgWg</recordid><startdate>20010501</startdate><enddate>20010501</enddate><creator>Naimi, B</creator><creator>Harrison, A</creator><creator>Cummins, M</creator><creator>Nongthomba, U</creator><creator>Clark, S</creator><creator>Canal, I</creator><creator>Ferrus, A</creator><creator>Sparrow, J C</creator><general>The American Society for Cell Biology</general><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><scope>5PM</scope></search><sort><creationdate>20010501</creationdate><title>A tropomyosin-2 mutation suppresses a troponin I myopathy in Drosophila</title><author>Naimi, B ; Harrison, A ; Cummins, M ; Nongthomba, U ; Clark, S ; Canal, I ; Ferrus, A ; Sparrow, J C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c373t-8e4107b984540fa68f1afd0123370afb9a6e83a5dbb90d0e5d0b08dbc5b7ad8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Behavior, Animal - physiology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila melanogaster - growth & development</topic><topic>Drosophila melanogaster - physiology</topic><topic>Flight, Animal - physiology</topic><topic>Humans</topic><topic>Larva - physiology</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Muscle Contraction - physiology</topic><topic>Muscle, Skeletal - physiology</topic><topic>Muscle, Skeletal - ultrastructure</topic><topic>Mutation, Missense - genetics</topic><topic>Phenotype</topic><topic>Sequence Alignment</topic><topic>Suppression, Genetic - genetics</topic><topic>Tropomyosin - genetics</topic><topic>Tropomyosin - metabolism</topic><topic>Troponin I - genetics</topic><topic>Troponin I - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Naimi, B</creatorcontrib><creatorcontrib>Harrison, A</creatorcontrib><creatorcontrib>Cummins, M</creatorcontrib><creatorcontrib>Nongthomba, U</creatorcontrib><creatorcontrib>Clark, S</creatorcontrib><creatorcontrib>Canal, I</creatorcontrib><creatorcontrib>Ferrus, A</creatorcontrib><creatorcontrib>Sparrow, J C</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Naimi, B</au><au>Harrison, A</au><au>Cummins, M</au><au>Nongthomba, U</au><au>Clark, S</au><au>Canal, I</au><au>Ferrus, A</au><au>Sparrow, J C</au><au>Pringle, John</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A tropomyosin-2 mutation suppresses a troponin I myopathy in Drosophila</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2001-05-01</date><risdate>2001</risdate><volume>12</volume><issue>5</issue><spage>1529</spage><epage>1539</epage><pages>1529-1539</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>A suppressor mutation, D53, of the held-up(2) allele of the Drosophila melanogaster Troponin I (wupA) gene is described. D53, a missense mutation, S185F, of the tropomyosin-2, Tm2, gene fully suppresses all the phenotypic effects of held-up(2), including the destructive hypercontraction of the indirect flight muscles (IFMs), a lack of jumping, the progressive myopathy of the walking muscles, and reductions in larval crawling and feeding behavior. The suppressor restores normal function of the IFMs, but flight ability decreases with age and correlates with an unusual, progressive structural collapse of the myofibrillar lattice starting at the center. The S185F substitution in Tm2 is close to a troponin T binding site on tropomyosin. Models to explain suppression by D53, derived from current knowledge of the vertebrate troponin-tropomyosin complex structure and functions, are discussed. The effects of S185F are compared with those of two mutations in residues 175 and 180 of human alpha-tropomyosin 1 which cause familial hypertrophic cardiomyopathy (HCM).</abstract><cop>United States</cop><pub>The American Society for Cell Biology</pub><pmid>11359941</pmid><doi>10.1091/mbc.12.5.1529</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Behavior, Animal - physiology Drosophila melanogaster - genetics Drosophila melanogaster - growth & development Drosophila melanogaster - physiology Flight, Animal - physiology Humans Larva - physiology Male Molecular Sequence Data Muscle Contraction - physiology Muscle, Skeletal - physiology Muscle, Skeletal - ultrastructure Mutation, Missense - genetics Phenotype Sequence Alignment Suppression, Genetic - genetics Tropomyosin - genetics Tropomyosin - metabolism Troponin I - genetics Troponin I - metabolism |
title | A tropomyosin-2 mutation suppresses a troponin I myopathy in Drosophila |
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