Nucleic Acids Research, Vol 26, Issue 12 2963-2970, Copyright © 1998 by Oxford University Press
F Rossi, E Labourier, IE Gallouzi, J Derancourt, E Allemand, G Divita and J Tazi
Human DNA topoisomerase I not only has DNA relaxing activity, but also
splicing factors phosphorylating activity. Topo I shows strong preference
for ATP as the phosphate donor. We used photoaffinity labeling with the ATP
analogue [alpha-32P] 8-azidoadenosine-5'- triphosphate combined with
limited proteolysis to characterize Topo I domains involved in ATP binding.
The majority of incorporated analogue was associated with two fragments
derived from N-terminal and C- terminal regions of Topo I, respectively.
However, mutational analysis showed that deletion of the first 138
N-terminal residues, known to be dispensable for topoisomerase activity,
did not change the binding of ATP or the kinase activity. In contrast,
deletion of 162 residues from the C-terminal domain was deleterious for ATP
binding, kinase and topoisomerase activities. Furthermore, a C-terminal
tyrosine 723 mutant lacking topoisomerase activity is still able to bind
ATP and to phosphorylate SF2/ASF, suggesting that the two functions of Topo
I can be separated. These findings argue in favor of the fact that Topo I
is a complex enzyme with a number of potential intra-cellular functions.
ARTICLES
The C-terminal domain but not the tyrosine 723 of human DNA topoisomerase I active site contributes to kinase activity
Institut de Genetique Moleculaire de Montpellier (IGM), UMR 5535 CNRS, Universite Montpellier II, CNRS 1919, route de Mende, F34293 Montpellier Cedex 5, France.
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