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Nucleic Acids Research, 1990, Vol. 18, No. 4 895-900
© 1990

MOLECULAR BIOLOGY

TcA, the putative transposase of the C.elegans Tc1 transposon, has an N-terminal DNA binding domain

Rianne F. Schukkink and Ronald H.A. Plasterk

The Netherlands Cancer Institute, Division of Chemical Carcinogenesis Plesrnanlaan 121, 1066CX Amsterdam, The Netherlands

Received November 2, 1989. Revised January 18, 1990. Accepted January 18, 1990.

Tc1 is a transposon present in several copies in the genome of all natural isolates of the nematode C.elegans; it is actively transposing in many strains. In those strains Tc1 insertion is the main cause of spontaneous mutations. The transposon contains one large ORF that we call TcA; we assume that the TcA protein is the transposase of id. We expressed TcA in E.coli, purified the protein and showed that it has a strong affinity for DNA (both single stranded and double stranded). A fusion protein of ß-galactosidase and TcA also exhibits DNA binding; deletion derivatives of this fusion protein were tested for DNA binding. A deletion of 39 amino acids at the N-terminal region of TcA abolishes the DNA binding, whereas a deletion of 108 C-terminal amino acids does not affect DNA binding. This shows that the DNA binding domain of TcA is near the N-terminal region. The DNA binding capacity of TcA supports the assumption that TcA is a transposase of Tc1.


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