Microbiology

Download PDF by W. Zillig, R. Schnabel, K. O. Stetter (auth.), M. Cooper, H.: Current Topics in Microbiology and Immunology

By W. Zillig, R. Schnabel, K. O. Stetter (auth.), M. Cooper, H. Eisen, W. Goebel, P. H. Hofschneider, H. Koprowski, F. Melchers, M. Oldstone, R. Rott, H. G. Schweiger, P. K. Vogt, I. Wilson (eds.)

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The enzyme together with the DNA ends, to which it would be attached, would then form a lock into which an intact duplex segment of the same or another DNA molecule could penetrate similar to what is envisaged for the relaxation reaction. Subsequent reclosure of the transient interruption would complete the topological linkage of DNA molecules. The reverse reaction of decatenation would proceed via the same route. The w-protein on one hand and the eukaryotic type I topoisomerases on the other have many properties in common, but they also differ in a variety of respects (see Table 2).

Thus, removal of about one-third of the native protein does not impair the enzymatic activity of the topoisomerase. This part of the protein molecule may conceivably serve additional functions which escape detection in the standard assays, such as interaction with other proteins in chromatin. No gross differences have been found for the reaction requirements of the eukaryotic type I enzymes of different biological origin. Although systematic comparisons have not been made, it is likely that these enzymes have basically common properties and act according to a unique mechanism.

1983). Poly(ADP)ribosyl transferase is known to modify a number of intracellular proteins, among them some, such as histones, which are located in the nucleus. It is generally believed that these modifications are regulative measures of the cell (MANDEL et al. 1982). Another covalent modification of topoisomerase I is phosphorylation. A phosphorylated topoisomerase I (molecular weight 110000) was detected in the nuclei of Novikoff ascites cells, HeLa and Namalwa cells, and fetal rat liver, but not in adult rat liver (DURBAN et al.

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