Azuma N, Yamaguchi Y, Handa H, Hayakawa M, Kanai A, Yamada M
Department of Ophthalmology, National Children's Hospital, Tokyo 154-8509, Japan.
Am J Hum Genet. 1999 Sep;65(3):656-63. doi: 10.1086/302529.
The PAX6 gene is involved in ocular morphogenesis, and PAX6 mutations have been detected in various types of ocular anomalies, including aniridia, Peters anomaly, corneal dystrophy, congenital cataract, and foveal hypoplasia. The gene encodes a transcriptional regulator that recognizes target genes through its paired-type DNA-binding domain. The paired domain is composed of two distinct DNA-binding subdomains, the N-terminal subdomain (NTS) and the C-terminal subdomain (CTS), which bind respective consensus DNA sequences. The human PAX6 gene produces two alternative splice isoforms that have the distinct structure of the paired domain. The insertion, into the NTS, of 14 additional amino acids encoded by exon 5a abolishes the DNA-binding activity of the NTS and unmasks the DNA-binding ability of the CTS. Thus, exon 5a appears to function as a molecular switch that specifies target genes. We ascertained a novel missense mutation in four pedigrees with Peters anomaly, congenital cataract, Axenfeldt anomaly, and/or foveal hypoplasia, which, to our knowledge, is the first mutation identified in the splice-variant region. A T-->A transition at the 20th nucleotide position of exon 5a results in a Val-->Asp (GTC-->GAC) substitution at the 7th codon of the alternative splice region. Functional analyses demonstrated that the V54D mutation slightly increased NTS binding and decreased CTS transactivation activity to almost half.
PAX6基因参与眼部形态发生,并且在各种类型的眼部异常中检测到PAX6突变,包括无虹膜、彼得斯异常、角膜营养不良、先天性白内障和黄斑发育不全。该基因编码一种转录调节因子,其通过其配对型DNA结合结构域识别靶基因。配对结构域由两个不同的DNA结合亚结构域组成,即N端亚结构域(NTS)和C端亚结构域(CTS),它们结合各自的共有DNA序列。人类PAX6基因产生两种具有不同配对结构域结构的可变剪接异构体。由外显子5a编码的14个额外氨基酸插入到NTS中,消除了NTS的DNA结合活性,并揭示了CTS的DNA结合能力。因此,外显子5a似乎起着指定靶基因的分子开关的作用。我们在四个患有彼得斯异常、先天性白内障、阿克森费尔德异常和/或黄斑发育不全的家系中确定了一个新的错义突变,据我们所知,这是在剪接变体区域中鉴定出的第一个突变。外显子5a第20个核苷酸位置的T→A转换导致可变剪接区域第7个密码子处的Val→Asp(GTC→GAC)取代。功能分析表明,V54D突变略微增加了NTS结合,并将CTS反式激活活性降低至几乎一半。