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
Hauptverfasser: Franz, G, Loukeris, T.G, Dialektaki, G, Thompson, C.R.L, Savakis, C
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container_end_page 4750
container_issue 11
container_start_page 4746
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 91
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.</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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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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