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小鼠h1-钙调蛋白基因的完整核苷酸序列、结构组织及一个可变剪接外显子

Complete nucleotide sequence, structural organization, and an alternatively spliced exon of mouse h1-calponin gene.

作者信息

Gao J, Hwang J M, Jin J P

机构信息

Department of Medical Biochemistry, University of Calgary Faculty of Medicine, Alberta, Canada.

出版信息

Biochem Biophys Res Commun. 1996 Jan 5;218(1):292-7. doi: 10.1006/bbrc.1996.0051.

Abstract

From a CC1.2 embryonic stem cell genomic library, we isolated and sequenced a 10.4-kb DNA segment (GenBank/EMBL Data Bank accession number L49022) containing the entire gene encoding mouse h1-calponin, an actin-associated smooth muscle-specific protein and a potential modulator of contraction. Sequence data revealed that there are seven exons and six introns in the h1-calponin gene. Determined by primer extension mapping of the RNA transcripts, the transcription of h1-calponin gene initiates at the same site in stomach, urinary bladder and pregnant uterus smooth muscles. The genomic organization suggests that the previously identified alpha- and beta-calponin isoforms are produced by splicing of exon 7 at two alternative acceptor sites. Isolation and structural characterization of the h1-calponin gene provides information to further investigate the expression regulation of this smooth muscle-specific gene.

摘要

我们从CC1.2胚胎干细胞基因组文库中分离并测序了一段10.4 kb的DNA片段(GenBank/EMBL数据库登录号L49022),该片段包含编码小鼠h1 - 钙调蛋白的完整基因,h1 - 钙调蛋白是一种与肌动蛋白相关的平滑肌特异性蛋白,也是收缩的潜在调节因子。序列数据显示,h1 - 钙调蛋白基因有7个外显子和6个内含子。通过对RNA转录本进行引物延伸定位确定,h1 - 钙调蛋白基因在胃、膀胱和妊娠子宫平滑肌中的转录起始于同一位置。基因组结构表明,先前鉴定的α - 和β - 钙调蛋白异构体是由外显子7在两个不同的剪接受体位点进行剪接产生的。h1 - 钙调蛋白基因的分离和结构表征为进一步研究这个平滑肌特异性基因的表达调控提供了信息。

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