MBE Advance Access originally published online on December 22, 2004
Molecular Biology and Evolution 2005 22(4):833-844; doi:10.1093/molbev/msi068
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Research Article |
Homologs of Drosophila P Transposons Were Mobile in Zebrafish but Have Been Domesticated in a Common Ancestor of Chicken and Human

* Laboratories of Genome Dynamics, Center of Anatomy and Cell Biology, Medical University of Vienna, Vienna, Austria; and
Children's Cancer Research Institute, Vienna, Austria
E-mail: sylvia.hagemann{at}meduniwien.ac.at.
A substantial fraction of vertebrate and invertebrate genomes is composed of mobile elements and their derivatives. One of the most intensively studied transposon families, the P elements of Drosophila, was thought to exist exclusively in the genomes of dipteran insects. Based on the data provided by the human genome project, in 2001 our group has identified a P elementhomologous sequence in the human genome. This P elementhomologous human gene, named Phsa, is 19,533 nucleotides long, comprises six exons and five introns, and encodes a protein of still unknown function with a length of 903 amino acid residues. The N-terminal THAP domain of the putative Phsa protein shows similarities to the site-specific DNA-binding domain of the Drosophila P element transposase. In the present study, FISH analysis and the screening of a human lambda genomic library revealed a single copy of Phsa located on the long arm of chromosome 4, upstream of a gene coding for the hypothetical protein DKFZp686L1814. The same gene arrangement was found for the homologous gene Pgga in the genome of chicken, thus, displaying Pgga at orthologous position on the long arm of chromosome 4. The single-copy gene status and the absence of terminal inverted repeats and target-site duplications indicate that Phsa and Pgga constitute domesticated stationary sequences. In contrast, a considerable number of P-homologous sequences with terminal inverted repeats and intact target-site duplications could be identified in zebrafish, strongly indicating that Pdre elements were mobile within the zebrafish genome. Pdre elements are the first P-like transposons identified in a vertebrate species. With respect to Phsa, gene expression studies showed that Phsa is expressed in a broad range of human tissues, suggesting that the putative Phsa protein plays a not yet understood but essential role in a specific metabolic pathway. We demonstrate that P-homologous DNA sequences occur in the genomes of 21 analyzed vertebrates but only as rudiments in the rodents. Finally, the evolutionary history of P elementhomologous vertebrate sequences is discussed in the context of the "molecular domestication" hypothesis versus the "source gene hypothesis."
Key Words: Drosophila P transposons Homo sapiens Danio rerio Gallus gallus THAP proteins molecular domestication
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
T.P. Zwaka Ronin and Caspases in Embryonic Stem Cells: A New Perspective on Regulation of the Pluripotent State Cold Spring Harb Symp Quant Biol, November 6, 2008; (2008) sqb.2008.73.007v1. [Abstract] [PDF] |
||||
![]() |
R. S. Linheiro and C. M. Bergman Testing the palindromic target site model for DNA transposon insertion using the Drosophila melanogaster P-element Nucleic Acids Res., November 1, 2008; 36(19): 6199 - 6208. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. Bessiere, C. Lacroix, S. Campagne, V. Ecochard, V. Guillet, L. Mourey, F. Lopez, J. Czaplicki, P. Demange, A. Milon, et al. Structure-Function Analysis of the THAP Zinc Finger of THAP1, a Large C2CH DNA-binding Module Linked to Rb/E2F Pathways J. Biol. Chem., February 15, 2008; 283(7): 4352 - 4363. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. K. Cowan, D. R. Hoen, D. J. Schoen, and T. E. Bureau MUSTANG Is a Novel Family of Domesticated Transposase Genes Found in Diverse Angiosperms Mol. Biol. Evol., October 1, 2005; 22(10): 2084 - 2089. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Clouaire, M. Roussigne, V. Ecochard, C. Mathe, F. Amalric, and J.-P. Girard The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity PNAS, May 10, 2005; 102(19): 6907 - 6912. [Abstract] [Full Text] [PDF] |
||||




