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小鼠精氨酸酶II基因的结构。

Structure of the murine arginase II gene.

作者信息

Shi O, Kepka-Lenhart D, Morris S M, O'Brien W E

机构信息

Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030, USA.

出版信息

Mamm Genome. 1998 Oct;9(10):822-4. doi: 10.1007/s003359900874.

Abstract

Mammals contain two genes encoding distinct isoforms of arginase (arginases I and II), both of which catalyze the conversion of arginine to ornithine and urea. However, their subcellular localization and tissue-specific patterns of expression are very different, indicating that they perform distinct physiologic roles. As an initial step in elucidating the regulation and physiologic roles of arginase II, this report describes the characterization of a mammalian arginase II gene. The murine arginase II gene contains eight exons like the arginase I gene. The six internal exons have intron/exon boundaries that are identical to the arginase I gene; however, exon three of the arginase II gene has obtained a three-base-pair insertion. The identity of the exon/intron boundaries is consistent with a gene duplication as the origin of the arginase isozymes with the small insertion occurring after the duplicative event. The promoter region of the arginase II gene, which bears no resemblance to that of the arginase I genes, contains numerous potential binding sites for enhancer and promoter elements but does not contain a TATA box.

摘要

哺乳动物含有两个编码精氨酸酶不同同工型(精氨酸酶I和精氨酸酶II)的基因,这两种酶都催化精氨酸转化为鸟氨酸和尿素。然而,它们的亚细胞定位和组织特异性表达模式非常不同,表明它们发挥着不同的生理作用。作为阐明精氨酸酶II的调节和生理作用的第一步,本报告描述了一种哺乳动物精氨酸酶II基因的特征。小鼠精氨酸酶II基因与精氨酸酶I基因一样,包含八个外显子。六个内部外显子具有与精氨酸酶I基因相同的内含子/外显子边界;然而,精氨酸酶II基因的第三个外显子有一个三碱基对的插入。外显子/内含子边界的一致性与基因复制一致,精氨酸酶同工型起源于此,小插入发生在复制事件之后。精氨酸酶II基因的启动子区域与精氨酸酶I基因的启动子区域没有相似之处,包含许多增强子和启动子元件的潜在结合位点,但不包含TATA框。

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