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

Luca Falciola, Alastair I H Murchie, David M J Lilley, Marco E. Bianchi

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)285-292
Number of pages8
JournalNucleic Acids Research
Volume22
Issue number3
Publication statusPublished - Feb 11 1994

ASJC Scopus subject areas

  • Genetics
  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Health, Toxicology and Mutagenesis
  • Toxicology
  • Genetics(clinical)

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    Falciola, L., Murchie, A. I. H., Lilley, D. M. J., & Bianchi, M. E. (1994). Mutational analysis of the DNA binding domain A of chromosomal protein HMG1. Nucleic Acids Research, 22(3), 285-292.