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. 1994 Feb 11;22(3):285–292. doi: 10.1093/nar/22.3.285

Mutational analysis of the DNA binding domain A of chromosomal protein HMG1.

L Falciola 1, A I Murchie 1, D M Lilley 1, M Bianchi 1
PMCID: PMC523578  PMID: 8127664

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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