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J. Biol. Chem., Vol. 269, Issue 40, 24523-24526, Oct, 1994
K Kimura, N Nozaki, M Saijo, A Kikuchi, M Ui and T Enomoto
Human cell lines express two genetically distinct isoforms of DNA
topoisomerase (topo II) II: topo II alpha (p170) and topo II beta (p180).
We detected a higher molecular weight form with an apparent molecular mass
of about 190 kDa in M phase-arrested HeLa cells (Kimura, K., Saijo, M., Ui,
M., and Enomoto, T. (1994) J. Biol. Chem. 269, 1173- 1176). In this study
we confirmed, using anti-topo II alpha and topo II beta monoclonal
antibodies, that this higher molecular weight form is topo II beta and
consists of doublet bands around 190 kDa. We confirmed that the doublet
bands constituted an M phase-specific phenomenon and were not an artifact
of the procedure used to accumulate mitotic cells. Digesting the
immunoprecipitated materials from mitotic cell extracts with alkaline
phosphatase resulted in the disappearance of the doublet bands and the
appearance of the 180-kDa band with the concomitant disappearance of 32P
label in the region of the doublet bands. Neither heat-inactivated alkaline
phosphatase nor phosphodiesterase affected the doublet bands and the 32P
label. Topo II beta in interphase cells was also phosphorylated, but the
shift in apparent molecular weight was very slight after alkaline
phosphatase digestion. Analysis of the labeled phosphoamino acids present
in topo II beta from M phase and logarithmically growing cells indicated
that phosphorylation occurred mainly on serine and fairly on threonine
residues in both topo II beta isoforms. These results indicated that topo
II beta is phosphorylated at specific sites in M phase, resulting in the
formation of the doublet bands.
Identification of the nature of modification that causes the shift of DNA topoisomerase II beta to apparent higher molecular weight forms in the M phase
Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
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