MOLECULAR-CLONING AND HETEROLOGOUS EXPRESSION OF AN ALTERNATIVELY SPLICED HUMAN MU CLASS GLUTATHIONE-S-TRANSFERASE TRANSCRIPT
MOLECULAR-CLONING AND HETEROLOGOUS EXPRESSION OF AN ALTERNATIVELY SPLICED HUMAN MU CLASS GLUTATHIONE-S-TRANSFERASE TRANSCRIPT
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DOI：
10.1042/bj2940373
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发表时间：
1993-09-01
影响因子：
4.1
通讯作者：
BOARD, PG
中科院分区：
文献类型：
--
作者：
ROSS, VL;BOARD, PG
从人睾丸文库中分离到两个编码新的Mu类谷胱甘肽S转移酶(GST)的基因。这两个克隆都是不完整的，似乎是选择性剪接的结果。一个克隆缺失编码外显子4的序列，另一个缺失编码外显子8的序列。从这两个克隆可以推导出上述未被描述的同工酶的完整序列。这是首次报道GST转录本中的选择性剪接，可能代表了这个多基因家族中的一种新的调控形式，或者是作为进化过程的一部分的非法转录和实验性选择性剪接。通过组合每个克隆的成分，构建了一个完整的cDNA，并在大肠杆菌中表达了编码的蛋白。总体而言，与所有已报道的人类Mu类GST同工酶相比，该重组酶的活性相对较低。
Two cDNA clones encoding a new Mu class glutathione S-transferase (GST) have been isolated from a human testis cDNA library. Both clones are incomplete and appear to result from alternative splicing. One clone is missing the sequence encoding exon 4 and the other is missing exon 8. The complete sequence of the previously undescribed isoenzyme can be deduced from the two cDNA clones. This is the first report of alternative splicing in a GST transcript and may represent either a novel form of regulation in this mutigene family or illegitimate transcription and experimental alternative splicing as part of the evolutionary process. By combining components from each clone a complete cDNA has been constructed and the encoded protein expressed in Escherichia coli. In general, the recombinant enzyme has relatively low activity when compared with all the previously described human Mu class GST isoenzymes.