Mobile Minos elements from Drosophila hydei encode a two-exon transposase with similarity to the paired DNA-binding domain.
AUTOR(ES)
Franz, G
RESUMO
Elements related to the Tc1-like Minos mobile element have been cloned from Drosophila hydei and sequenced. Southern blot and sequence analyses show that (i) the elements are actively transposing in the Drosophila hydei germ line, (ii) they are characterized by a striking degree of sequence and size homogeneity, and (iii) like Tc1, they insert at a TA dinucleotide that is probably duplicated during the process. The nucleotide sequences of two elements, Minos-2 and Minos-3, differ at only one position from each other and contain two nonoverlapping open reading frames that are separated by a putative 60-nucleotide intron. The amino-terminal part of the Minos putative transposase shows sequence similarity to the paired DNA-binding domain. Forced transcription of a modified Minos element that was introduced into the Drosophila melanogaster germ line by P element-mediated transformation resulted in the production of accurately spliced polyadenylylated RNA molecules. It is proposed that Minos-2 and/or Minos-3 may encode an active transposase containing an amino-terminal DNA-binding domain that is distantly related to the paired DNA-binding domain.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=43865Documentos Relacionados
- Structural domains in phage Mu transposase: identification of the site-specific DNA-binding domain.
- Drosophila and vertebrate myb proteins share two conserved regions, one of which functions as a DNA-binding domain.
- The essential DNA-binding protein sap1 of Schizosaccharomyces pombe contains two independent oligomerization interfaces that dictate the relative orientation of the DNA-binding domain.
- Mutational analysis of the att DNA-binding domain of phage Mu transposase.
- Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA