Subunit interaction in the CCAAT-binding heteromeric complex is mediated by a very short alpha-helix in HAP2

We dissected the domain of HAP2 that mediates subunit association in the heteromeric CCAAT-binding complex, first by genetic mutational analysis and then by structural studies. The mutational data suggest that a very short region in HAP2 mediates protein-protein association and that the structure of...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1994-04, Vol.91 (8), p.3009-3013
Main Authors: Xing, Y.Y, Zhang, S.G, Olesen, J.T, Rich, A, Guarente, L
Format: Article
Language:English
Subjects:
ADN
Amino Acid Sequence
Amino acids
Biochemistry
Biological and medical sciences
CCAAT-Binding Factor
Circular Dichroism
DNA
Fundamental and applied biological sciences. Psychology
Fungal Proteins - chemistry
Fungal Proteins - metabolism
Gels
Genetic mutation
Lactates
Leucine Zippers
Macromolecular Substances
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Molecules
MUTACION INDUCIDA
Mutagenesis
Mutagenesis, Site-Directed
MUTANT
MUTANTES
MUTATION PROVOQUEE
Protein Binding
Protein Structure, Secondary
PROTEINAS
PROTEINE
Proteins
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - chemistry
Structure-Activity Relationship
Transcription Factors - chemistry
Transcription Factors - metabolism
Transcription. Transcription factor. Splicing. Rna processing
Yeasts
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Summary:We dissected the domain of HAP2 that mediates subunit association in the heteromeric CCAAT-binding complex, first by genetic mutational analysis and then by structural studies. The mutational data suggest that a very short region in HAP2 mediates protein-protein association and that the structure of this domain is likely to be an alpha-helix. The CD analyses of a 15-residue synthetic oligopeptide covering this region confirm this surmise. The oligopeptide indeed formed an unusually thermal stable alpha-helix in aqueous solution. Eight amino acids that lie along one face of this helix, including three arginines, are found to be critical for protein-protein association. The partner that interacts with this helical motif is likely to be another subunit in the HAP complex, since the CCAAT-binding factor is shown to contain one molecule of HAP2. Our results suggest that very short regions in proteins can encode precise structures and mediate stable and specific protein-protein recognition and interactions
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.8.3009