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完整鸡δ-晶体蛋白cDNA的序列

Sequence of a complete chicken delta-crystallin cDNA.

作者信息

Nickerson J M, Piatigorsky J

出版信息

Proc Natl Acad Sci U S A. 1984 May;81(9):2611-5. doi: 10.1073/pnas.81.9.2611.

DOI:10.1073/pnas.81.9.2611
PMID:6585817
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC345119/
Abstract

A full-length chicken delta-crystallin cDNA (p delta Cr17) was cloned and subjected to sequence analysis. The cDNA was shown to be full-length by both primer extension and S1 and mung bean nuclease experiments. Thus, the complete amino acid sequence of delta-crystallin is now available. The delta-crystallin polypeptide has a molecular mass of 48,542 daltons, as expected from its behavior on NaDodSO4/polyacrylamide gels. delta-Crystallin has one tryptophan, no cysteines, a prevalence of leucines (15%), and a paucity of aromatic residues. High alpha-helical content throughout the protein was predicted from the amino acid sequence. Nucleic acid sequence analysis suggests that delta-crystallin gene 1 encodes the mRNA that gave rise to the cDNA clone. These data provide a basis for the detailed analysis of the two delta-crystallin genes.

摘要

克隆了一个全长鸡δ-晶体蛋白cDNA(pδCr17)并进行了序列分析。通过引物延伸以及S1和绿豆核酸酶实验证明该cDNA是全长的。因此,现在可以获得δ-晶体蛋白完整的氨基酸序列。δ-晶体蛋白多肽的分子量为48,542道尔顿,这与其在十二烷基硫酸钠/聚丙烯酰胺凝胶上的行为预期一致。δ-晶体蛋白有一个色氨酸,没有半胱氨酸,亮氨酸含量较高(15%),芳香族残基较少。根据氨基酸序列预测整个蛋白质具有较高的α-螺旋含量。核酸序列分析表明,δ-晶体蛋白基因1编码产生该cDNA克隆的mRNA。这些数据为详细分析两个δ-晶体蛋白基因提供了基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86ce/345119/7ff5ceed2ef4/pnas00610-0020-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86ce/345119/d96746b4d702/pnas00610-0020-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86ce/345119/7ff5ceed2ef4/pnas00610-0020-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86ce/345119/d96746b4d702/pnas00610-0020-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86ce/345119/7ff5ceed2ef4/pnas00610-0020-b.jpg

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1
Sequence of a complete chicken delta-crystallin cDNA.完整鸡δ-晶体蛋白cDNA的序列
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本文引用的文献

1
Electrophoretic and immunoelectrophoretic studies on the soluble proteins in the developing lens of birds.鸟类发育晶状体中可溶性蛋白质的电泳和免疫电泳研究。
Exp Eye Res. 1962 Jun;1:310-6. doi: 10.1016/s0014-4835(62)80017-7.
2
The molecular structure and stability of the eye lens: x-ray analysis of gamma-crystallin II.眼晶状体的分子结构与稳定性:γ-晶状体蛋白II的X射线分析
Nature. 1981 Feb 26;289(5800):771-7. doi: 10.1038/289771a0.
3
Chicken lens crystallin DNA sequences show at least two delta-crystallin genes.鸡晶状体晶状体蛋白DNA序列显示至少有两个δ-晶状体蛋白基因。
在移植的鸡晶状体上皮细胞中,由小鼠αA-晶状体蛋白基因的5'侧翼序列促进的氯霉素乙酰转移酶基因的晶状体特异性表达。
Proc Natl Acad Sci U S A. 1985 Apr;82(8):2334-8. doi: 10.1073/pnas.82.8.2334.
4
Gene sharing by delta-crystallin and argininosuccinate lyase.δ-晶状体蛋白与精氨琥珀酸裂解酶的基因共享
Proc Natl Acad Sci U S A. 1988 May;85(10):3479-83. doi: 10.1073/pnas.85.10.3479.
5
In vivo competition of delta-crystallin gene expression by DNA fragments containing a GC box.含GC框的DNA片段在体内对δ-晶体蛋白基因表达的竞争作用
Mol Cell Biol. 1986 Nov;6(11):4130-2. doi: 10.1128/mcb.6.11.4130-4132.1986.
6
Crystallin gene expression and lentoid body formation in quail embryo neuroretina cultures transformed by the oncogenic retrovirus Mill Hill 2 or Rous sarcoma virus.致癌逆转录病毒米尔希尔2号或劳斯肉瘤病毒转化的鹌鹑胚胎神经视网膜培养物中的晶状体蛋白基因表达及类晶状体小体形成
Mol Cell Biol. 1986 Nov;6(11):3704-10. doi: 10.1128/mcb.6.11.3704-3710.1986.
7
The chicken delta 1-crystallin gene promoter: binding of transcription factor(s) to the upstream G+C-rich region is necessary for promoter function in vitro.鸡δ1-晶状体蛋白基因启动子:转录因子与富含G+C的上游区域结合是其体外启动子功能所必需的。
Proc Natl Acad Sci U S A. 1986 May;83(10):3131-5. doi: 10.1073/pnas.83.10.3131.
8
Nucleotide sequence of a chicken delta-crystallin gene.鸡δ-晶体蛋白基因的核苷酸序列。
Nucleic Acids Res. 1985 Mar 11;13(5):1593-606. doi: 10.1093/nar/13.5.1593.
9
Conservation of delta-crystallin gene structure between ducks and chickens.鸭和鸡之间δ-晶体蛋白基因结构的保守性。
J Mol Evol. 1987;25(4):308-17. doi: 10.1007/BF02603115.
Nature. 1980 Mar 20;284(5753):234-8. doi: 10.1038/284234a0.
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The nucleic acid and deduced protein sequence of cDNA clones for delta-crystallin of the chicken lens.
FEBS Lett. 1982 Aug 2;144(2):289-92. doi: 10.1016/0014-5793(82)80656-x.
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Degradation of delta-crystallin mRNA in the lens fiber cells of the chicken.鸡晶状体纤维细胞中δ-晶状体蛋白mRNA的降解
Dev Biol. 1982 Jul;92(1):60-5. doi: 10.1016/0012-1606(82)90150-6.
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Primary structure of the bovine beta-crystallin Bp chain. Internal duplication and homology with gamma-crystallin.牛β-晶状体蛋白Bp链的一级结构。内部重复及与γ-晶状体蛋白的同源性。
Eur J Biochem. 1981 Dec;121(1):83-91. doi: 10.1111/j.1432-1033.1981.tb06433.x.
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Lens differentiation in vertebrates. A review of cellular and molecular features.脊椎动物的晶状体分化。细胞和分子特征综述。
Differentiation. 1981;19(3):134-53. doi: 10.1111/j.1432-0436.1981.tb01141.x.
8
Eye-lens proteins: the three-dimensional structure of beta-crystallin predicted from monomeric gamma-crystallin.眼晶状体蛋白:由单体γ-晶状体蛋白预测的β-晶状体蛋白的三维结构。
FEBS Lett. 1981 Oct 12;133(1):9-16. doi: 10.1016/0014-5793(81)80460-7.
9
Evolution and diversity of the crystallins. Nucleotide sequence of a beta-crystallin mRNA from the mouse lens.晶状体蛋白的进化与多样性。来自小鼠晶状体的β-晶状体蛋白mRNA的核苷酸序列。
J Biol Chem. 1982 Aug 10;257(15):9064-71.
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Tissue-specific expression of a cloned chick delta-crystallin gene in mouse cells.克隆的鸡δ-晶体蛋白基因在小鼠细胞中的组织特异性表达。
Nature. 1983 Feb 3;301(5899):440-2. doi: 10.1038/301440a0.