Feldmar S et al. 1991
- Authors:
Feldmar S. Kunze R.
- Title:
The ORFa protein, the putative transposase of maize transposable element
Ac, has a basic DNA binding domain.
- Reference location:
EMBO Journal. 10(13):4003-10, 1991 Dec.
- Abstract:
Ac encodes the 807 amino acid ORFa protein which binds specifically to
multiple AAACGG motifs that are subterminally located in both ends of Ac.
The wild-type ORFa protein and a number of deletion and amino acid
exchange mutants were expressed in Escherichia coli, renatured and used
for mobility shift assays. At least 136 amino acids from the N-terminus
and 537 C-terminal amino acids may be removed from the ORFa protein
without destroying the DNA binding domain, whereas a protein starting at
amino acid 189 is DNA binding deficient. Certain basic amino acids between
positions 190 and 200 are essential for DNA binding, as their substitution
with uncharged amino acids leads to the loss of this function. The DNA
binding domain of ORFa protein has an overall basic character, but no
obvious sequence homology to any other known DNA binding protein. The
homologies to the major open reading frames of transposable elements Tam3
from Antirrhinum majus and Hobo from Drosophila are found between the
C-terminal two thirds of the three proteins. The ORFa protein forms
discrete complexes with target DNA that appear, depending on the protein
concentration, as a 'ladder' of bands on gels, indicating the occupation
of target DNA by multiple ORFa protein molecules.
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