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Two novel mutations of the AIRE protein affecting its homodimerization properties
Author(s) -
Meloni A.,
Fiorillo E.,
Corda D.,
Perniola R.,
Cao A.,
Rosatelli M. C.
Publication year - 2005
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/humu.9309
Subject(s) - biology , genetics , mutation , heterozygote advantage , compound heterozygosity , microbiology and biotechnology , gene , allele
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. © 2005 Wiley‐Liss, Inc.