Mobile Minos elements from Drosophila hydei encode a two-exon transposase with similarity to the paired DNA-binding domain
Elements related to the Tc1-like Minos mobile element have been cloned from Drosophila hydei and sequenced. Southern blot and sequence analyses show that (i) the elements are actively transposing in the Drosophila hydei germ line, (ii) they are characterized by a striking degree of sequence and size...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1994-05, Vol.91 (11), p.4746-4750 |
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creator | Franz, G Loukeris, T.G Dialektaki, G Thompson, C.R.L Savakis, C |
description | Elements related to the Tc1-like Minos mobile element have been cloned from Drosophila hydei and sequenced. Southern blot and sequence analyses show that (i) the elements are actively transposing in the Drosophila hydei germ line, (ii) they are characterized by a striking degree of sequence and size homogeneity, and (iii) like Tc1, they insert at a TA dinucleotide that is probably duplicated during the process. The nucleotide sequences of two elements, Minos-2 and Minos-3, differ at only one position from each other and contain two nonoverlapping open reading frames that are separated by a putative 60-nucleotide intron. The amino-terminal part of the Minos putative transposase shows sequence similarity to the paired DNA-binding domain. Forced transcription of a modified Minos element that was introduced into the Drosophila melanogaster germ line by P element-mediated transformation resulted in the production of accurately spliced polyadenylylated RNA molecules. It is proposed that Minos-2 and/or Minos-3 may encode an active transposase containing an amino-terminal DNA-binding domain that is distantly related to the paired DNA-binding domain. |
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Southern blot and sequence analyses show that (i) the elements are actively transposing in the Drosophila hydei germ line, (ii) they are characterized by a striking degree of sequence and size homogeneity, and (iii) like Tc1, they insert at a TA dinucleotide that is probably duplicated during the process. The nucleotide sequences of two elements, Minos-2 and Minos-3, differ at only one position from each other and contain two nonoverlapping open reading frames that are separated by a putative 60-nucleotide intron. The amino-terminal part of the Minos putative transposase shows sequence similarity to the paired DNA-binding domain. Forced transcription of a modified Minos element that was introduced into the Drosophila melanogaster germ line by P element-mediated transformation resulted in the production of accurately spliced polyadenylylated RNA molecules. It is proposed that Minos-2 and/or Minos-3 may encode an active transposase containing an amino-terminal DNA-binding domain that is distantly related to the paired DNA-binding domain.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.91.11.4746</identifier><identifier>PMID: 8197129</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>ADN ; Amino Acid Sequence ; Amino acids ; Animals ; Base Sequence ; Binding Sites ; Cellular biology ; Deoxyribonucleic acid ; DNA ; DNA Transposable Elements ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Drosophila ; Drosophila - enzymology ; Drosophila - genetics ; Drosophila hydei ; ENZIMAS ; ENZYME ; Exons ; GENE ; GENES ; Genetic transposition ; Insects ; Introns ; Molecular Sequence Data ; Nucleic acids ; Nucleotidyltransferases - genetics ; Nucleotidyltransferases - metabolism ; Open reading frames ; PROTEINAS ; PROTEINE ; Proteins ; Repetitive Sequences, Nucleic Acid ; Ribosomal DNA ; RNA Splicing ; SECUENCIA NUCLEICA ; Sequence Homology, Amino Acid ; SEQUENCE NUCLEIQUE ; Terminal repeat sequences ; Transcription, Genetic ; Transposases ; Transposons</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1994-05, Vol.91 (11), p.4746-4750</ispartof><rights>Copyright 1994 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences May 24, 1994</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4546-6c3378d36af09efbea215398f10eb53aad2b33236d6d9d20ff63803282ede9dc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/91/11.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2364846$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2364846$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8197129$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Franz, G</creatorcontrib><creatorcontrib>Loukeris, T.G</creatorcontrib><creatorcontrib>Dialektaki, G</creatorcontrib><creatorcontrib>Thompson, C.R.L</creatorcontrib><creatorcontrib>Savakis, C</creatorcontrib><title>Mobile Minos elements from Drosophila hydei encode a two-exon transposase with similarity to the paired DNA-binding domain</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Elements related to the Tc1-like Minos mobile element have been cloned from Drosophila hydei and sequenced. Southern blot and sequence analyses show that (i) the elements are actively transposing in the Drosophila hydei germ line, (ii) they are characterized by a striking degree of sequence and size homogeneity, and (iii) like Tc1, they insert at a TA dinucleotide that is probably duplicated during the process. The nucleotide sequences of two elements, Minos-2 and Minos-3, differ at only one position from each other and contain two nonoverlapping open reading frames that are separated by a putative 60-nucleotide intron. The amino-terminal part of the Minos putative transposase shows sequence similarity to the paired DNA-binding domain. Forced transcription of a modified Minos element that was introduced into the Drosophila melanogaster germ line by P element-mediated transformation resulted in the production of accurately spliced polyadenylylated RNA molecules. It is proposed that Minos-2 and/or Minos-3 may encode an active transposase containing an amino-terminal DNA-binding domain that is distantly related to the paired DNA-binding domain.</description><subject>ADN</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Cellular biology</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA Transposable Elements</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila</subject><subject>Drosophila - enzymology</subject><subject>Drosophila - genetics</subject><subject>Drosophila hydei</subject><subject>ENZIMAS</subject><subject>ENZYME</subject><subject>Exons</subject><subject>GENE</subject><subject>GENES</subject><subject>Genetic transposition</subject><subject>Insects</subject><subject>Introns</subject><subject>Molecular Sequence Data</subject><subject>Nucleic acids</subject><subject>Nucleotidyltransferases - genetics</subject><subject>Nucleotidyltransferases - metabolism</subject><subject>Open reading frames</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Proteins</subject><subject>Repetitive Sequences, Nucleic Acid</subject><subject>Ribosomal DNA</subject><subject>RNA Splicing</subject><subject>SECUENCIA NUCLEICA</subject><subject>Sequence Homology, Amino Acid</subject><subject>SEQUENCE NUCLEIQUE</subject><subject>Terminal repeat sequences</subject><subject>Transcription, Genetic</subject><subject>Transposases</subject><subject>Transposons</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAURiMEKkNhjYQAWSxglalfcWyJTdXyklpYQNeWE9_MeJTYqZ2hHX49HmYYURaw8uI735XvPUXxlOA5wTU7Gb1Jc0XmhMx5zcW9YkawIqXgCt8vZhjTupSc8ofFo5RWGGNVSXxUHEmiakLVrPhxGRrXA7p0PiQEPQzgp4S6GAZ0HkMK49L1Bi03FhwC3wYLyKDpJpRwGzyaovFpDMkkQDduWqLkhsxHN23QFNC0BDQaF8Gi88-nZeO8dX6BbBiM84-LB53pEzzZv8fF1ft3384-lhdfPnw6O70oW15xUYqWsVpaJkyHFXQNGEoqpmRHMDQVM8bShjHKhBVWWYq7TjCJGZUULCjbsuPi7W7uuG4GsG1eMJpej9ENJm50ME7fTbxb6kX4rjmTosr11_t6DNdrSJMeXGqh742HsE66FhVRhMn_gkRIpQhlGXz1F7gK6-jzDTTFhGEpOc_QyQ5qs4UUoTt8mGC9Va-36rUimhC9VZ8bL_7c88DvXef85T7fFn-ndwa8-Segu3XfT3A7ZfL5jlylKcQDmiVw-WvQs13cmaDNIrqkr76qKkvJ6_0ElabWEA</recordid><startdate>19940524</startdate><enddate>19940524</enddate><creator>Franz, G</creator><creator>Loukeris, T.G</creator><creator>Dialektaki, G</creator><creator>Thompson, C.R.L</creator><creator>Savakis, C</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19940524</creationdate><title>Mobile Minos elements from Drosophila hydei encode a two-exon transposase with similarity to the paired DNA-binding domain</title><author>Franz, G ; Loukeris, T.G ; Dialektaki, G ; Thompson, C.R.L ; Savakis, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4546-6c3378d36af09efbea215398f10eb53aad2b33236d6d9d20ff63803282ede9dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>ADN</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Cellular biology</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA Transposable Elements</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Drosophila</topic><topic>Drosophila - enzymology</topic><topic>Drosophila - genetics</topic><topic>Drosophila hydei</topic><topic>ENZIMAS</topic><topic>ENZYME</topic><topic>Exons</topic><topic>GENE</topic><topic>GENES</topic><topic>Genetic transposition</topic><topic>Insects</topic><topic>Introns</topic><topic>Molecular Sequence Data</topic><topic>Nucleic acids</topic><topic>Nucleotidyltransferases - genetics</topic><topic>Nucleotidyltransferases - metabolism</topic><topic>Open reading frames</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>Proteins</topic><topic>Repetitive Sequences, Nucleic Acid</topic><topic>Ribosomal DNA</topic><topic>RNA Splicing</topic><topic>SECUENCIA NUCLEICA</topic><topic>Sequence Homology, Amino Acid</topic><topic>SEQUENCE NUCLEIQUE</topic><topic>Terminal repeat sequences</topic><topic>Transcription, Genetic</topic><topic>Transposases</topic><topic>Transposons</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Franz, G</creatorcontrib><creatorcontrib>Loukeris, T.G</creatorcontrib><creatorcontrib>Dialektaki, G</creatorcontrib><creatorcontrib>Thompson, C.R.L</creatorcontrib><creatorcontrib>Savakis, C</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Franz, G</au><au>Loukeris, T.G</au><au>Dialektaki, G</au><au>Thompson, C.R.L</au><au>Savakis, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mobile Minos elements from Drosophila hydei encode a two-exon transposase with similarity to the paired DNA-binding domain</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1994-05-24</date><risdate>1994</risdate><volume>91</volume><issue>11</issue><spage>4746</spage><epage>4750</epage><pages>4746-4750</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Elements related to the Tc1-like Minos mobile element have been cloned from Drosophila hydei and sequenced. Southern blot and sequence analyses show that (i) the elements are actively transposing in the Drosophila hydei germ line, (ii) they are characterized by a striking degree of sequence and size homogeneity, and (iii) like Tc1, they insert at a TA dinucleotide that is probably duplicated during the process. The nucleotide sequences of two elements, Minos-2 and Minos-3, differ at only one position from each other and contain two nonoverlapping open reading frames that are separated by a putative 60-nucleotide intron. The amino-terminal part of the Minos putative transposase shows sequence similarity to the paired DNA-binding domain. Forced transcription of a modified Minos element that was introduced into the Drosophila melanogaster germ line by P element-mediated transformation resulted in the production of accurately spliced polyadenylylated RNA molecules. It is proposed that Minos-2 and/or Minos-3 may encode an active transposase containing an amino-terminal DNA-binding domain that is distantly related to the paired DNA-binding domain.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8197129</pmid><doi>10.1073/pnas.91.11.4746</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
subjects | ADN Amino Acid Sequence Amino acids Animals Base Sequence Binding Sites Cellular biology Deoxyribonucleic acid DNA DNA Transposable Elements DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Drosophila Drosophila - enzymology Drosophila - genetics Drosophila hydei ENZIMAS ENZYME Exons GENE GENES Genetic transposition Insects Introns Molecular Sequence Data Nucleic acids Nucleotidyltransferases - genetics Nucleotidyltransferases - metabolism Open reading frames PROTEINAS PROTEINE Proteins Repetitive Sequences, Nucleic Acid Ribosomal DNA RNA Splicing SECUENCIA NUCLEICA Sequence Homology, Amino Acid SEQUENCE NUCLEIQUE Terminal repeat sequences Transcription, Genetic Transposases Transposons |
title | Mobile Minos elements from Drosophila hydei encode a two-exon transposase with similarity to the paired DNA-binding domain |
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