The Ancient mariner Sails Again: Transposition of the Human Hsmar1 Element by a Reconstructed Transposase and Activities of the SETMAR Protein on Transposon Ends

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Published inMolecular and Cellular Biology Vol. 27; no. 12; pp. 4589 - 4600
Main Authors Miskey, Csaba, Papp, Balázs, Mátés, Lajos, Sinzelle, Ludivine, Keller, Heiko, Izsvák, Zsuzsanna, Ivics, Zoltán
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.06.2007
Taylor & Francis
Subjects
Amino Acid Sequence
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Computer Simulation
Consensus Sequence
Danio rerio
DNA Transposable Elements - genetics
DNA Transposable Elements - physiology
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Evolution, Molecular
Genes, Reporter
Histone-Lysine N-Methyltransferase - chemistry
Histone-Lysine N-Methyltransferase - genetics
Histone-Lysine N-Methyltransferase - metabolism
Humans
Luciferases - metabolism
Models, Biological
Molecular Sequence Data
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Phylogeny
Primates
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Transposases - genetics
Transposases - metabolism
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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList Hsmar1, one of the two subfamilies of mariner transposons in humans, is an ancient element that entered the primate genome lineage approximately 50 million years ago. Although Hsmar1 elements are inactive due to mutational damage, one particular copy of the transposase gene has apparently been under selection. This transposase coding region is part of the SETMAR gene, in which a histone methylatransferase SET domain is fused to an Hsmar1 transposase domain. A phylogenetic approach was taken to reconstruct the ancestral Hsmar1 transposase gene, which we named Hsmar1-Ra. The Hsmar1-Ra transposase efficiently mobilizes Hsmar1 transposons by a cut-and-paste mechanism in human cells and zebra fish embryos. Hsmar1-Ra can also mobilize short inverted-repeat transposable elements (MITEs) related to Hsmar1 (MiHsmar1), thereby establishing a functional relationship between an Hsmar1 transposase source and these MITEs. MiHsmar1 excision is 2 orders of magnitude more efficient than that of long elements, thus providing an explanation for their high copy numbers. We show that the SETMAR protein binds and introduces single-strand nicks into Hsmar1 inverted-repeat sequences in vitro. Pathway choices for DNA break repair were found to be characteristically different in response to transposon cleavage mediated by Hsmar1-Ra and SETMAR in vivo. Whereas nonhomologous end joining plays a dominant role in repairing excision sites generated by the Hsmar1-Ra transposase, DNA repair following cleavage by SETMAR predominantly follows a homology-dependent pathway. The novel transposon system can be a useful tool for genome manipulations in vertebrates and for investigations into the transpositional dynamics and the contributions of these elements to primate genome evolution.
Hsmar1, one of the two subfamilies of mariner transposons in humans, is an ancient element that entered the primate genome lineage similar to 50 million years ago. Although Hsmar1 elements are inactive due to mutational damage, one particular copy of the transposase gene has apparently been under selection. This transposase coding region is part of the SETMAR gene, in which a histone methylatransferase SET domain is fused to an Hsmar1 transposase domain. A phylogenetic approach was taken to reconstruct the ancestral Hsmar1 transposase gene, which we named Hsmar1-Ra. The Hsmar1-Ra transposase efficiently mobilizes Hsmar1 transposons by a cut-and-paste mechanism in human cells and zebra fish embryos. Hsmar1-Ra can also mobilize short inverted-repeat transposable elements (MITEs) related to Hsmar1 (MiHsmar1), thereby establishing a functional relationship between an Hsmar1 transposase source and these MITEs. MiHsmar1 excision is 2 orders of magnitude more efficient than that of long elements, thus providing an explanation for their high copy numbers. We show that the SETMAR protein binds and introduces single-strand nicks into Hsmar1 inverted-repeat sequences in vitro. Pathway choices for DNA break repair were found to be characteristically different in response to transposon cleavage mediated by Hsmar1-Ra and SETMAR in vivo. Whereas nonhomologous end joining plays a dominant role in repairing excision sites generated by the Hsmar1-Ra transposase, DNA repair following cleavage by SETMAR predominantly follows a homology-dependent pathway. The novel transposon system can be a useful tool for genome manipulations in vertebrates and for investigations into the transpositional dynamics and the contributions of these elements to primate genome evolution.
Hsmar1 , one of the two subfamilies of mariner transposons in humans, is an ancient element that entered the primate genome lineage ∼50 million years ago. Although Hsmar1 elements are inactive due to mutational damage, one particular copy of the transposase gene has apparently been under selection. This transposase coding region is part of the SETMAR gene, in which a histone methylatransferase SET domain is fused to an Hsmar1 transposase domain. A phylogenetic approach was taken to reconstruct the ancestral Hsmar1 transposase gene, which we named Hsmar1-Ra . The Hsmar1-Ra transposase efficiently mobilizes Hsmar1 transposons by a cut-and-paste mechanism in human cells and zebra fish embryos. Hsmar1-Ra can also mobilize short inverted-repeat transposable elements (MITEs) related to Hsmar1 ( MiHsmar1 ), thereby establishing a functional relationship between an Hsmar1 transposase source and these MITEs. MiHsmar1 excision is 2 orders of magnitude more efficient than that of long elements, thus providing an explanation for their high copy numbers. We show that the SETMAR protein binds and introduces single-strand nicks into Hsmar1 inverted-repeat sequences in vitro. Pathway choices for DNA break repair were found to be characteristically different in response to transposon cleavage mediated by Hsmar1-Ra and SETMAR in vivo. Whereas nonhomologous end joining plays a dominant role in repairing excision sites generated by the Hsmar1-Ra transposase, DNA repair following cleavage by SETMAR predominantly follows a homology-dependent pathway. The novel transposon system can be a useful tool for genome manipulations in vertebrates and for investigations into the transpositional dynamics and the contributions of these elements to primate genome evolution.
Hsmar1, one of the two subfamilies of mariner transposons in humans, is an ancient element that entered the primate genome lineage ∼50 million years ago. Although Hsmar1 elements are inactive due to mutational damage, one particular copy of the transposase gene has apparently been under selection. This transposase coding region is part of the SETMAR gene, in which a histone methylatransferase SET domain is fused to an Hsmar1 transposase domain. A phylogenetic approach was taken to reconstruct the ancestral Hsmar1 transposase gene, which we named Hsmar1-Ra. The Hsmar1-Ra transposase efficiently mobilizes Hsmar1 transposons by a cut-and-paste mechanism in human cells and zebra fish embryos. Hsmar1-Ra can also mobilize short inverted-repeat transposable elements (MITEs) related to Hsmar1 (MiHsmar1), thereby establishing a functional relationship between an Hsmar1 transposase source and these MITEs. MiHsmar1 excision is 2 orders of magnitude more efficient than that of long elements, thus providing an explanation for their high copy numbers. We show that the SETMAR protein binds and introduces single-strand nicks into Hsmar1 inverted-repeat sequences in vitro. Pathway choices for DNA break repair were found to be characteristically different in response to transposon cleavage mediated by Hsmar1-Ra and SETMAR in vivo. Whereas nonhomologous end joining plays a dominant role in repairing excision sites generated by the Hsmar1-Ra transposase, DNA repair following cleavage by SETMAR predominantly follows a homology-dependent pathway. The novel transposon system can be a useful tool for genome manipulations in vertebrates and for investigations into the transpositional dynamics and the contributions of these elements to primate genome evolution.
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Author Zsuzsanna Izsvák
Heiko Keller
Csaba Miskey
Ludivine Sinzelle
Balázs Papp
Lajos Mátés
Zoltán Ivics
AuthorAffiliation Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany, 1 Faculty of Life Sciences, The University of Manchester, Manchester M13 9PT, United Kingdom, 2 Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, 6726 Szeged, Hungary 3
AuthorAffiliation_xml – name: Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany, 1 Faculty of Life Sciences, The University of Manchester, Manchester M13 9PT, United Kingdom, 2 Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, 6726 Szeged, Hungary 3
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  surname: Miskey
  fullname: Miskey, Csaba
  organization: Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany
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  surname: Papp
  fullname: Papp, Balázs
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  surname: Mátés
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  organization: Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany
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  surname: Sinzelle
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  givenname: Zoltán
  surname: Ivics
  fullname: Ivics, Zoltán
  organization: Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany
BackLink https://www.ncbi.nlm.nih.gov/pubmed/17403897$$D View this record in MEDLINE/PubMed
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Corresponding author. Mailing address: Max Delbruck Center for Molecular Medicine, Robert Rössle Str. 10, D-13092 Berlin, Germany. Phone: (49) 30 9406-2546. Fax: (49) 30 9406-2547. E-mail: zivics@mdc-berlin.de
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Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Hsmar1, one of the two subfamilies of mariner transposons in humans, is an ancient element that entered the primate genome lineage ∼50 million years ago....
Hsmar1, one of the two subfamilies of mariner transposons in humans, is an ancient element that entered the primate genome lineage approximately 50 million...
Hsmar1, one of the two subfamilies of mariner transposons in humans, is an ancient element that entered the primate genome lineage similar to 50 million years...
Hsmar1 , one of the two subfamilies of mariner transposons in humans, is an ancient element that entered the primate genome lineage ∼50 million years ago....
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SourceType Open Access Repository
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StartPage 4589
SubjectTerms Amino Acid Sequence
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Computer Simulation
Consensus Sequence
Danio rerio
DNA Transposable Elements - genetics
DNA Transposable Elements - physiology
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Evolution, Molecular
Genes, Reporter
Histone-Lysine N-Methyltransferase - chemistry
Histone-Lysine N-Methyltransferase - genetics
Histone-Lysine N-Methyltransferase - metabolism
Humans
Luciferases - metabolism
Models, Biological
Molecular Sequence Data
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Phylogeny
Primates
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Transposases - genetics
Transposases - metabolism
Title The Ancient mariner Sails Again: Transposition of the Human Hsmar1 Element by a Reconstructed Transposase and Activities of the SETMAR Protein on Transposon Ends
URI http://mcb.asm.org/content/27/12/4589.abstract
https://www.tandfonline.com/doi/abs/10.1128/MCB.02027-06
https://www.ncbi.nlm.nih.gov/pubmed/17403897
https://search.proquest.com/docview/19773289
https://search.proquest.com/docview/70557734
https://pubmed.ncbi.nlm.nih.gov/PMC1900042
Volume 27
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