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1982) and BEEN et al. (1984) (for further details see p. 80). In a study on base-specific inhibition of calf thymus topoisomerases, DARBY and VOSBERG (1985) recently observed that the relaxation of supercoiled DNA by topoisomerase I is effectively blocked if dGMP in the DNA is replaced by a phosphorothioate dGMP (dGMPaS). Other base-specific substitutions are much less effective. In considering earlier results about inhibition by poly(dG) or poly(rG) (PRELL and VOSBERG 1980) and the strikingly infrequent appearance of dGMP within the consensus sequence for cleavage, one might speculate that dGMP or G-containing sequences are involved in DNA recognition by topoisomerase remote from the cleavage site.

Properties of Other Bacterial Type I Topoisomerases. A new type I topoisomerase in E. coli, called topoisomerase III, was recently described in two independent reports (DEAN et al. 1982; SRIVENUGOPAL et al. 1984). This enzyme is a single polypeptide with a molecular weight of 74000. It changes linking numbers in steps of one. It differs from the co-protein in its requirement for K + in addition to Mg2+ for optimal activity and in its affinity for novobiocin-Sepharose. Positive supercoils are not relaxed.

After isolation of these proteins from sodium dodecyl sulfate (SDS) polyacrylamide gels and reactivation (according to HAGER and BRUGESS 1980), all five showed topoisomerase activity (SCHMITT et al. 1984). A multiplicity of catalytically active forms of eukaryotic type I topoisomerases from a variety of sources has now been well documented (see TRASK and MULLER 1983; Lm 1983; TRICOLI and KOWALSKI 1983; MARTIN et al. 1983; ISHII et al. 1983). -P. Vosberg in the catalytic behavior of the two proteins could be detected (Lm and MILLER 1981).

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