Isolation and nucleotide sequence analysis of a cloned cDNA encoding the beta-subunit of bovine follicle-stimulating hormone.

Isolation and nucleotide sequence analysis of a cloned cDNA encoding the beta-subunit of bovine follicle-stimulating hormone.
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编码牛卵泡刺激素β亚基的克隆cDNA的分离和核苷酸序列分析。

DOI:
10.1089/dna.1986.5.363
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发表时间:
1986
期刊:
DNA (Mary Ann Liebert, Inc.)
影响因子:
--
通讯作者:
Beck,A
Beck,A
中科院分区:
--
文献类型:
--
作者:
Maurer,RA;Beck,A

文献摘要

被引文献

相似文献

从噬菌体lambda gt11牛垂体cDNA文库中分离到两个不同的含有牛促卵泡激素(FSH-β) β亚基序列的cDNA。测定了两个克隆的完整核苷酸序列,组合序列代表了FSH-β mRNA的大部分。该组合序列包含46个5 '未翻译序列和387个编码序列。该编码序列预测成熟牛FSH-β的氨基末端前体片段为19个氨基酸,随后是110个氨基酸序列。cDNA序列显示存在一个长3 '的非翻译区,包含1295个碱基,随后是一个代表mRNA的poly(a)部分的片段。因此,cdna的组合序列表明FSH-β mRNA的最小大小为1.7 kb。对牛垂体mRNA中存在的FSH-β序列的分析表明,存在一个大小约为2.0 kb的mRNA。这种明显的差异可能是由于在mRNA的3 '端存在数百个核苷酸的聚(a)链。将cDNA预测的氨基酸序列与已知的几种不同物种FSH β-亚基的氨基酸序列进行比较,表明该蛋白具有高度保守性。
Two different cDNAs containing sequences coding for the β-subunit of bovine follicle stimulating hormone (FSH-β) have been isolated from a phage lambda gt11 bovine pituitary cDNA library. The complete nucleotide sequence of both clones was determined, and the combined sequence represents most of FSH-β mRNA. The combined sequence contains 46 nucleotides of 5′-untranslated sequence followed by 387 nucleotides of coding sequence. The coding sequence predicts a 19-amino-acid amino-terminal precursor segment followed by the 110-amino-acid sequence of mature bovine FSH-β. The cDNA sequence demonstrates the presence of a long 3′-untranslated region containing 1295 bases followed by a segment representing the poly(A) portion of the mRNA. Thus, the combined sequence of the cDNAs suggests a minimal size of 1.7 kb for FSH-β mRNA. Analysis of FSH-β sequences present in bovine pituitary mRNA demonstrated the presence of an mRNA with a size of about 2.0 kb. This apparent discrepancy is probably due to the presence of a several-hundred nucleotide tract of poly(A) at the 3′ terminus of the mRNA. Comparison of the amino acid sequence predicted from the cDNA with the known amino acid sequence of the β-subunit of FSH from several different species demonstrates that the protein has been highly conserved.