A novel and major isoform of tyrosine hydroxylase in Drosophila is generated by alternative RNA processing.
A novel and major isoform of tyrosine hydroxylase in Drosophila is generated by alternative RNA processing.
复制标题
DOI：
10.1016/s0021-9258(18)47231-6
复制
发表时间：
1994-10
期刊：
影响因子：
--
通讯作者：
S. Birman;Bruce Morgan;M. Anzivino;J. Hirsh
中科院分区：
文献类型：
--
作者：
S. Birman;Bruce Morgan;M. Anzivino;J. Hirsh
我们报告果蝇酪氨酸羟化酶蛋白的两种亚型是通过选择性剪接的外显子编码的。主要亚型（II 型）在氨基末端调节域中包含 71 个氨基酸的新型酸性延伸，这可能会改变酪氨酸羟化酶蛋白的调节特性。次要亚型（I 型）对应于先前报道的 cDNA 序列。我们还报告了果蝇酪氨酸羟化酶（DTH）基因的结构及其转录物的多样性和组织定位。通过选择性剪接和聚腺苷酸化，从单个初级转录物中产生至少三种类型的 DTH mRNA。 II 型 mRNA 是果蝇中最丰富的酪氨酸羟化酶转录物，主要存在于整个发育阶段的皮下组织中。 I 型 mRNA 仅存在于中枢神经系统中，是其主要形式。由于多聚腺苷酸化差异，在 CNS 中检测到的 DTH 转录物包含比皮下组织中表达的转录物更长的 3'-非翻译区域。相反，两种组织中的 DTH 基因转录使用相同的起始位点。这些结果显示了 DTH 转录本中意想不到的多样性，并指出了中枢神经系统和皮下组织中酪氨酸羟化酶活性差异调节的可能机制。
We report that two isoforms of Drosophila tyrosine hydroxylase protein are encoded via alternatively spliced exons. The major isoform (Type II) contains a novel acidic extension of 71 amino acids in the amino-terminal regulatory domain, which is likely to alter the regulatory properties of the tyrosine hydroxylase protein. The minor isoform (Type I) corresponds to the cDNA sequence reported previously. We also report the structure of the Drosophila tyrosine hydroxylase (DTH) gene and the diversity and tissue localization of its transcripts. At least three types of DTH mRNA are generated from a single primary transcript through alternative splicing and polyadenylation. Type II mRNA is the most abundant tyrosine hydroxylase transcript in Drosophila and is found predominantly in the hypoderm throughout all stages of development. Type I mRNA is present only in the CNS, where it is the primary form. The DTH transcripts detected in the CNS contain a longer 3'-untranslated region than the transcript expressed in the hypoderm, due to differential polyadenylation. In contrast, the same start site is used for DTH gene transcription in both tissues. These results show unexpected diversity in the DTH transcripts and point out possible mechanisms for differential regulation of tyrosine hydroxylase activity in the CNS and in the hypoderm.