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Title:
Origin of the paired domain | Discover Developmental Biology
Description:
Pax proteins play a diverse role in early animal development and contain the characteristic paired domain, consisting of two conserved helix-turn-helix motifs. In many Pax proteins the paired domain is fused to a second DNA binding domain of the paired-like homeobox family. By amino acid sequence alignments, secondary structure prediction, 3D-structure comparison, and phylogenetic reconstruction, we analyzed the relationship between Pax proteins and members of the Tc1 family of transposases, which possibly share a common ancestor with Pax proteins. We suggest that the DNA binding domain of an ancestral transposase (proto-Pax transposase) was fused to a homeodomain shortly after the emergence of metazoans about one billion years ago. Using the transposase sequences as an outgroup we reexamined the early evolution of the Pax proteins. Our novel evolutionary scenario features a single homeobox capturing event and an early duplication of Pax genes before the divergence of porifera, indicating a more diverse role of Pax proteins in primitive animals than previously expected.
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Keywords {🔍}
pax, article, proteins, domain, evolution, privacy, cookies, paired, content, information, publish, research, search, transposase, data, journal, development, genes, download, breitling, gerber, role, early, dna, homeobox, family, gene, human, discover, optional, analysis, personal, parties, policy, find, track, origin, sequence, cite, pdf, manuscript, rainer, explore, diverse, characteristic, fused, binding, common, september, related,
Topics {✒️}
conserved helix-turn-helix motifs dna binding domain characteristic paired domain privacy choices/manage cookies early evolution related subjects evolution aims proto-pax transposase early animal development pax gene family pax proteins main content log european economic area secondary structure prediction 3d-structure comparison billion years ago evolutionary scenario features germany e-mail conditions privacy policy article breitling accepting optional cookies pax genes paired domain homeobox family journal finder publish search search pax6 mutations article cite information common ancestor ancestral transposase transposase sequences privacy policy personal data books a optional cookies manage preferences data protection essential cookies cookies skip de tel journal publish tc1 family early duplication social media varying standards november 2000 volume 210 diverse role phylogenetic reconstruction possibly share
Schema {🗺️}
WebPage:
mainEntity:
headline:Origin of the paired domain
description:Pax proteins play a diverse role in early animal development and contain the characteristic paired domain, consisting of two conserved helix-turn-helix motifs. In many Pax proteins the paired domain is fused to a second DNA binding domain of the paired-like homeobox family. By amino acid sequence alignments, secondary structure prediction, 3D-structure comparison, and phylogenetic reconstruction, we analyzed the relationship between Pax proteins and members of the Tc1 family of transposases, which possibly share a common ancestor with Pax proteins. We suggest that the DNA binding domain of an ancestral transposase (proto-Pax transposase) was fused to a homeodomain shortly after the emergence of metazoans about one billion years ago. Using the transposase sequences as an outgroup we reexamined the early evolution of the Pax proteins. Our novel evolutionary scenario features a single homeobox capturing event and an early duplication of Pax genes before the divergence of porifera, indicating a more diverse role of Pax proteins in primitive animals than previously expected.
datePublished:
dateModified:
pageStart:644
pageEnd:650
sameAs:https://doi.org/10.1007/s004270000106
keywords:
Keywords Pax protein
Paired domain
Homeobox
Transposase
Evolution
Developmental Biology
Evolutionary Biology
Zoology
Animal Genetics and Genomics
Cell Biology
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1432-041X
0949-944X
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author:
name:Rainer Breitling
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name:GSF-National Research Center for Environment and Health, Institute of Experimental Genetics, 85764 Neuherberg, Germany e-mail: [email protected] Tel.: +49-89-31873229, Fax: +49-89-31873225
address:
name:GSF-National Research Center for Environment and Health, Institute of Experimental Genetics, 85764 Neuherberg, Germany e-mail: [email protected] Tel.: +49-89-31873229, Fax: +49-89-31873225, , DE
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headline:Origin of the paired domain
description:Pax proteins play a diverse role in early animal development and contain the characteristic paired domain, consisting of two conserved helix-turn-helix motifs. In many Pax proteins the paired domain is fused to a second DNA binding domain of the paired-like homeobox family. By amino acid sequence alignments, secondary structure prediction, 3D-structure comparison, and phylogenetic reconstruction, we analyzed the relationship between Pax proteins and members of the Tc1 family of transposases, which possibly share a common ancestor with Pax proteins. We suggest that the DNA binding domain of an ancestral transposase (proto-Pax transposase) was fused to a homeodomain shortly after the emergence of metazoans about one billion years ago. Using the transposase sequences as an outgroup we reexamined the early evolution of the Pax proteins. Our novel evolutionary scenario features a single homeobox capturing event and an early duplication of Pax genes before the divergence of porifera, indicating a more diverse role of Pax proteins in primitive animals than previously expected.
datePublished:
dateModified:
pageStart:644
pageEnd:650
sameAs:https://doi.org/10.1007/s004270000106
keywords:
Keywords Pax protein
Paired domain
Homeobox
Transposase
Evolution
Developmental Biology
Evolutionary Biology
Zoology
Animal Genetics and Genomics
Cell Biology
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name:GSF-National Research Center for Environment and Health, Institute of Experimental Genetics, 85764 Neuherberg, Germany e-mail: [email protected] Tel.: +49-89-31873229, Fax: +49-89-31873225, , DE
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