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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Mutations in yeast HAP2/HAP3 define a hybrid CCAAT box binding domain.

We describe a detailed genetic analysis of the DNA-binding regions in the HAP2/HAP3 CCAAT-binding heteromeric complex. The DNA-binding domain of HAP2 is shown to be a 21 residue region containing three critical histidines and three critical arginines. Mutation of an arginine at position 199 to leucine alters the DNA-binding specificity of the complex to favor CCAAC over CCAAT. Residues in HAP3 that are critical for DNA-binding comprise a short, seven amino acid region. Three different mutations in the HAP2 DNA- binding domain are suppressed by a mutation in the HAP3 DNA-binding domain. This HAP3 mutation also suppresses mutations in a different region of HAP2 which promotes subunit assembly of the complex. These findings suggest that short regions of HAP2 and HAP3 comprise a hybrid DNA-binding domain and that this domain can help hold the two subunits together in the CCAAT-binding complex.[1]


  1. Mutations in yeast HAP2/HAP3 define a hybrid CCAAT box binding domain. Xing, Y., Fikes, J.D., Guarente, L. EMBO J. (1993) [Pubmed]
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