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

      Nucleic Acids Research

      Animals, Base Sequence, Consensus Sequence, DNA-Binding Proteins, chemistry, genetics, High Mobility Group Proteins, Structure-Activity Relationship, Mammals, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment, Sequence Homology, Amino Acid, Amino Acid Sequence

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          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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          Journal
          8127664
          523578

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