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非洲爪蟾FIII/YY1的特性研究,FIII/YY1是一种与L1和L14核糖体蛋白基因的第一个外显子结合的保守锌指蛋白。

Characterization of FIII/YY1, a Xenopus laevis conserved zinc-finger protein binding to the first exon of L1 and L14 ribosomal protein genes.

作者信息

Pisaneschi G, Ceccotti S, Falchetti M L, Fiumicino S, Carnevali F, Beccari E

机构信息

Dipartimento di Genetica e Biologia Molecolare, Università di Roma La Sapienza, Italy.

出版信息

Biochem Biophys Res Commun. 1994 Dec 15;205(2):1236-42. doi: 10.1006/bbrc.1994.2797.

DOI:10.1006/bbrc.1994.2797
PMID:7802655
Abstract

The cDNA coding for the Xenopus laevis homolog of the transcriptional activator/repressor protein delta/YY1 was isolated from a lambda gt11 oocyte cDNA library. The deduced aminoacid sequence shows that the four zinc fingers of the DNA binding domain are 99% conserved when compared to the mouse (delta) and 95% to the human (YY1) proteins, while differences are found in the N-terminal region. In particular, the long run of consecutive glycines and histidines of delta and YY1 is missing. The protein, named FIII/YY1, was overexpressed into Xenopus oocytes from the cDNA under direction of the L14 rp-promoter and found to share antigenic and DNA-binding properties with the oocyte endogenous protein binding to the first exon of the X.laevis ribosomal protein genes (rp-genes) L1 and L14.

摘要

从λgt11卵母细胞cDNA文库中分离出编码非洲爪蟾转录激活因子/抑制因子蛋白δ/YY1同源物的cDNA。推导的氨基酸序列表明,与小鼠(δ)相比,DNA结合结构域的四个锌指有99%的保守性,与人类(YY1)蛋白相比有95%的保守性,而在N端区域存在差异。特别是,δ和YY1中连续的甘氨酸和组氨酸的长序列缺失。该蛋白名为FIII/YY1,在L14 rp启动子的指导下从cDNA在非洲爪蟾卵母细胞中过表达,发现它与结合到非洲爪蟾核糖体蛋白基因(rp基因)L1和L14第一外显子的卵母细胞内源性蛋白具有抗原性和DNA结合特性。

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