Nucleic Acids Research, Vol 27, Issue 11 2408-2415, Copyright © 1999 by Oxford University Press
DJ Wells
Tdd-4 is the first DNA transposon to be isolated from Dictyostelium
discoideum. This element was isolated by insertion into a target plasmid.
Two classes of elements were identified which include a 3.8 kb version and
a 3.4 kb deleted version. Sequence analysis reveals that the 145 bp
inverted terminal repeats contain the 5'-TGellipsisCA-3' conserved terminal
dinucleotides found in prokaryotic transposons and integrated LTR
retroelement DNA sequences. Tdd-4 open reading frames are assembled by
removal of six introns. Introns 1-5 conform to the GT- AG rule, whereas
intron 6 appears to be an AT-AA intron. Also, intron 6 undergoes an
alternative 5' splicing reaction. The alternatively spliced region encodes
15 tandem SPXX repeats that are proposed to function as a DNA binding
motif. By analogy to other transposons that encode two proteins from the
same gene, the full-length Tdd-4 protein is the putative transposase and
the truncated Tdd-4 protein is the putative transposition inhibitor.
Protein database searches demonstrate Tdd-4 encoded proteins are unique for
a DNA element by containing similarities to retroviral/retrotransposon
integrases. The putative Tdd- 4 transposase contains the same structural
relationship as integrases by possessing an N-terminal HHCC motif, a
central DDE motif and a C- terminal DNA-binding domain composed of the SPXX
motif.
ARTICLES
Tdd-4, a DNA transposon of Dictyostelium that encodes proteins similar to LTR retroelement integrases
Program in Molecular Biology, Department of Biology, Utah State University, Logan, UT 84322, USA. dwells@atlas.niaid.nih.gov
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