Jule from the fish Xiphophorus is the first complete vertebrate Ty3/Gypsy retrotransposon from the Mag family.
Jule is the second complete long-terminal-repeat (LTR) Ty3/Gypsy retrotransposon identified to date in vertebrates. Jule, first isolated from the poeciliid fish Xiphophorus maculatus, is 4.8 kb in length, is flanked by two 202-bp LTRs, and encodes Gag (structural core protein) and Pol (protease, reverse transcriptase, RNase H, and integrase, in that order) but no envelope. There are three to four copies of Jule per haploid genome in X. maculatus. Two of them are located in a subtelomeric region of the sex chromosomes, where they are associated with the Xmrk receptor tyrosine kinase genes, of which oncogenic versions are responsible for the formation of hereditary melanoma in Xiphophorus. One almost intact copy of Jule was found in the first intron of the X-chromosomal allele of the Xmrk proto-oncogene, and a second, more corrupted copy is present only 56 nt downstream of the polyadenylation signal of the Xmrk oncogene. Jule-related elements were detected by Southern blot hybridization with less than 10 copies per haploid genome in numerous other poeciliids, as well as in more divergent fishes, including the medakafish Oryzias latipes and the tilapia Oreochromis niloticus. Database searches also identified Jule-related sequences in the zebrafish Danio rerio and in both genome project pufferfishes, Fugu rubripes and Tetraodon nigroviridis. Phylogenetic analysis revealed that Jule is the first member of the Mag family of Ty3/Gypsy retrotransposons described to date in vertebrates. This family includes the silkworm Mag and sea urchin SURL retrotransposons, as well as sequences from the nematode Caenorhabditis elegans. Additional related elements were identified in the genomes of the malaria mosquito Anopheles gambiae and the nematode Ascaris lumbricoides. Phylogeny of Mag-related elements suggested that the Mag family of retrotransposons is polyphyletic and is constituted of several ancient lineages that diverged before their host genomes more than 600 MYA.
Volff
J N
JN
Physiological Chemistry I, Biocenter, University of Würzburg, Am Hubland, D-97074 Würzburg, Germany. volff@biozentrum.uni-wuerzburg.de
Körting
C
C
Altschmied
J
J
Duschl
J
J
Sweeney
K
K
Wichert
K
K
Froschauer
A
A
Schartl
M
M
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D004247:DNA / Q000032:analysis*; D019143:Evolution, Molecular; D015683:Gene Products, gag / Q000235:genetics*; D015684:Gene Products, pol / Q000235:genetics*; D016678:Genome; D019426:Integrases / Q000235:genetics*; D008969:Molecular Sequence Data; D010802:Phylogeny; D011036:Poecilia / Q000235:genetics*; D011518:Proto-Oncogene Proteins / Q000235:genetics; D018626:Retroelements; D017386:Sequence Homology, Amino Acid; D014960:X Chromosome; D014998:Y Chromosome
D015683:Gene Products, gag; D015684:Gene Products, pol; D011518:Proto-Oncogene Proteins; D018626:Retroelements; D004247:DNA; D019426:Integrases