Binding to four-way junction DNA: a common property of architectural proteins?

^a Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331–7305, USA
^b Institute of Genetics, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria

Proteins that can be shown to strongly bind in vitro to the four-way (Holliday) junction DNA include not only the obvious candidates such as enzymes involved in recombination, but also a remarkably diverse group of seemingly unrelated proteins. These include the HMG1 box proteins, members of the HMGI-Y family, winged helix proteins (including linker histones), the SWI/SNF complex, and some totally unrelated prokaryotic proteins. What these proteins seem to share is a propensity to bind to bent DNA, to bend DNA upon binding, and/or to preferentially interact with DNA crossings. Thus, they appear to be, in the main, architectural proteins, although some (like the SWI/SNF complex) have very specific functional roles as well. Perhaps because they bind to or promote the formation of particular DNA structures, the four-way junction binding proteins are frequently interchangeable in cellular function. Furthermore, since a given kind of structure can be recognized by many different protein motifs, it is not surprising that apparently unrelated proteins can fall into such a single functional class.—Zlatanova, J., van Holde, K. Binding to four-way junction DNA: a common property of architectural proteins? FASEB J. 12, 421–431 (1998)

Key Words: HMG box • HU • IHF • linker histones • SWI/SNF

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