Human mutation, 2005-03, Vol.25 (3), p.319-319
2005
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- Autor(en) / Beteiligte
- Titel
- Two novel mutations of the AIRE protein affecting its homodimerization properties
- Ist Teil von
- Human mutation, 2005-03, Vol.25 (3), p.319-319
- Ort / Verlag
- Hoboken: Wiley Subscription Services, Inc., A Wiley Company
- Erscheinungsjahr
- 2005
- Quelle
- Wiley Online Library Journals Frontfile Complete
- Beschreibungen/Notizen
- 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. © 2005 Wiley‐Liss, Inc.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1059-7794eISSN: 1098-1004DOI: 10.1002/humu.9309Titel-ID: cdi_proquest_miscellaneous_17799602
- Format
- –
- Schlagworte
- Adult, AIRE, AIRE Protein, Amino Acid Sequence, Child, Dimerization, Female, Heterozygote, homodimerization, HSR domain, Humans, Italy, Molecular Sequence Data, Mutagenesis, Site-Directed, mutation, Mutation, Missense, Point Mutation, Polyendocrinopathies, Autoimmune - genetics, Protein Interaction Mapping, Protein Structure, Tertiary, Sequence Deletion, Sequence Homology, Amino Acid, Sicily, Transcription Factors - chemistry, Transcription Factors - genetics, Two-Hybrid System Techniques