Nucleic Acids Research, 1994, Vol. 22, No. 3 285-292
© 1994
MOLECULAR BIOLOGY |
Mutational analysis of the DNA binding domain A of chromosomal protein HMG1
1DIBIT, San Raffaele Scientific Institute via Olgettina 58 20132 Milan, Italy 2Department of Biochemistry, The University Dundee DD1 4HN, UK 3Dipartimento di Genetica e di Biologia dei Microrganismi, Universitá di Milano via Celoria 26, 20133 Milan, Italy
*To whom correspondence should be addressed at DIBIT, San Raffaele Scientific Institute, via Olgettina 58, 20132 Milan, Italy
Received November 9, 1993. Accepted January 10, 1994.
We have mutated several residues of the first of the two HMG-boxes of mammalian HMG1. Some mutants cannot be produced in Escherichia coli, suggesting that the peptide fold Is grossly disrupted. A few others can be produced efficiently and have normal DNA binding affinity and specificity; however, they are more sensitive towards heating and chaotropic agents than the wild type polypeptide. Significantly, the mutation of the single most conserved residue in the rather diverged HMG-box family falls in this ‘in vitro temperature-sensitive’ category, rather than In the non-folded category. Finally, two other mutants have reduced DNA binding affinity but unchanged binding specificity. Overall, it appears that whenever the HMG-box can fold, it will interact specifically with kinked DNA.
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