Isolation, differential splicing and protein expression of a DNase on the human X chromosome.
Isolation, differential splicing and protein expression of a DNase on the human X chromosome.
复制标题
人类 X 染色体上 DNase 的分离、差异剪接和蛋白质表达。
DOI：
--
复制
发表时间：
1996
影响因子：
12.4
通讯作者：
H. Zentgraf
中科院分区：
文献类型：
--
作者：
J. Coy;I. Velhagen;R. Himmele;H. Delius;A. Poustka;H. Zentgraf
系统搜索在人体组织中差异表达的基因，结果分离出编码与DNA酶I具有高度同源性的蛋白质的基因。除了最近描述的cDNA序列（Parrish等人，1995），我们已经分离了在5'非编码区中选择性剪接的转录物。该基因位于Xq 28中QM和XAP-2基因之间，编码302个氨基酸的蛋白质，与人DNA酶I具有39%的同一性。除了在核苷酸和氨基酸水平上具有高度同源性外，DNase I和DNase X的大多数外显子-内含子边界是相同的，这表明这两个基因可能是从共同的祖先进化而来的。通过在诱导型细菌系统中表达重组蛋白并检测DNA酶活性，验证了预测的功能。与DNA酶I相反，全长35 kdal蛋白的18 kdal氨基末端片段表现出DNA酶活性。
A systematic search for genes differentially expressed in human tissues resulted in the isolation of a gene encoding a protein with high homology to DNase I. In addition to the recently described cDNA sequence (Parrish et al., 1995) we have isolated a transcript, alternatively spliced in the 5' noncoding region. The gene is located between the QM and the XAP-2 gene in Xq28 and encodes a 302 amino acid protein with 39% identity to human DNase I. Besides a high homology at the nucleotide and amino acid level, most exon-intron boundaries of DNase I and DNase X are identical, indicating that both genes may have evolved from a common ancestor. The predicted function was verified by expression of a recombinant protein in an inducible bacterial system and detection of DNase activity. In contrast to DNase I a 18 kdal amino terminal fragment of the full length 35 kdal protein exhibited DNase activity.