Cover: Atomic force microscopy shows that a recombinant fusion protein containing a fragment of the zinc finger protein RIP60 is able to condense bacterial artifical chromosomes and other large DNA molecules by DNA looping. As shown in the diagram, the protein first binds at dispersed sites, and then mediates DNA looping by protein–protein interactions. Montigny et al., in this issue [Nucleic Acids Res. (2001), 29, 1982-1988], have used condensation by RIP60 to increase the efficiency of transfer of large DNA molecules into mammalian cells. Cover art by Per-Ola Arvidsson.
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