title: Two novel mutations of the AIRE protein affecting its homodimerization properties.
abstract: We report two novel mutations, c.230T>C (p.F77S) and c.64_69del (p.V22_D23del) within the HSR domain of the AIRE protein in two patients of Italian descent affected by APECED. Both mutations were found in the compound heterozygous state respectively with c.994+5G>T and c.232T>A (p.W78R). With the two-hybrid assay in the yeast system we found that constructs containing the two mutations fail to interact with the wild-type protein. These findings indicate that both mutations negatively affected the homodimerization properties of the AIRE protein, thereby leading to a defective function.
authors.affiliation: Istituto di Neurogenetica e Neurofarmacologia, National Research Council, Cagliari, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Meloni
authors.forename: E
authors.initials: E
authors.lastname: Fiorillo
authors.forename: D
authors.initials: D
authors.lastname: Corda
authors.forename: R
authors.initials: R
authors.lastname: Perniola
authors.forename: A
authors.initials: A
authors.lastname: Cao
authors.forename: M C
authors.initials: MC
authors.lastname: Rosatelli
mesh_terms: D000328:Adult; D000595:Amino Acid Sequence; D002648:Child; D019281:Dimerization; D005260:Female; D006579:Heterozygote; D006801:Humans; D007558:Italy; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D020125:Mutation, Missense; D017354:Point Mutation; D016884:Polyendocrinopathies, Autoimmune / Q000235:genetics*; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D012802:Sicily; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics*; D020798:Two-Hybrid System Techniques; D000096927:AIRE Protein
chemical_list: D014157:Transcription Factors; D000096927:AIRE Protein