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. 2007 Sep 5;104(37):14670–14675. doi: 10.1073/pnas.0701989104

Table 1.

Comparison of type I topoisomerases

Properties Type
IA IB IC
Phylogenetic distribution Archaea, Prokarya, and Eukarya (3) Prokarya, Eukarya, and some eukaryotic viruses (3) Archaea* (3)
Cleavage polarity 5′ (25) 3′ (3) 3′ (1)
Substrate DNA Negatively supercoiled DNA (25) Positively and negatively supercoiled DNA (3) Positively and negatively supercoiled DNA (1)
Mg2+ dependence Yes (25) No (3) No (1)
Change in linking number Strictly in steps of +1 (9) In steps of n (〈ΔLk〉 ≈19 at zero force) (11) In steps of n (〈ΔLk〉 ≈12 at zero angular velocity in 40% glycerol)
Force dependence on linking number change No (9, 26) Yes (11) Yes
Relaxation velocity 0.0023 μm/sec (26) 4.1§–6.7 μm/sec (11) 3.0 μm/sec
Structural properties Toroidal shape; binds ssDNA along a groove and accepts passing strand in central hole (6, 27); structural and mechanistic similarities to type II enzymes (22) Concave shape; surrounds DNA in a clamp-like manner; structural similarities to tyrosine recombinases suggest a common ancestor (21, 28) Unique fold that includes a large positively charged groove containing a helix–turn–helix motif; some of the active site residues are found in the helix–turn–helix motif (5)
Mechanism Enzyme-bridged strand passage (79) Swiveling or ″controlled rotation″ (10, 11) Constrained swiveling

*So far found in M. kandleri isolates only.

Some type IA enzymes can relax positively supercoiled DNA at high temperatures (29).

T. maritima topo IA (26).

§Human topo IB (0.2 pN) (11).

Vaccinia topo IB (0.2 pN) (11).

Measured at a force of 0.5 pN.

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