Nucleic Acids Research, 1994, Vol. 22, No. 6 1044-1051
© 1994
MOLECULAR BIOLOGY |
DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain
trostokrová1Institute of Biophysics, Czech Academy of Sciences Královopolská 135, 612 65 Brno 1Institute of Molecular Genetics, Czech Academy of Sciences Flemingovo nám. 2, 166 37 Prague, Czech Republic 2Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge Tennis Court Road, Cambridge CB2 1QW, UK
*To whom correspondence should be addressed
Received December 3, 1993. Revised February 10, 1994. Accepted February 10, 1994.
We have compared HMG1 with the product of tryptic removal of its acidic C-terminal domain termed HMG3, which contains two ‘HMG-box’ DNA-blnding domains. (I) HMG3 has a higher affinity for DNA than HMG1. (II) Both HMG1 and HMG3 supercoil circular DNA in the presence of topoisomerase I. Supercolling by HMG3 is the same at 
50 mM and 150 mM ionic strength, as is its affinity for DNA, whereas supercoiling by HMG1 is less at 150 mM than at 50 mM ionic strength although its affinity for DNA is unchanged, showing that the acidic C-termlnal tail represses supercolllng at the higher ionic strength, (lll) Electron microscopy shows that HMG3 at a low protein:DNA input ratio (1:1 w/w; r = 1), and HMG1 at a 6-fold higher ratio, cause looping of relaxed circular DNA at 150 mM ionic strength. Ollgomerlc protein ‘beads’ are apparent at the bases of the loops and at cross-overs of DNA duplexes, (iv) HMG3 at high input ratios (r = 6), but not HMG1, causes DNA compaction without distortion of the B-form. The two HMG-box domains of HMG1 are thus capable of manipulating DNA by looping, compaction and changes in topology. The acidic C-tail down-regulates these effects by modulation of the DNA-blndlng properties.
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