CHARACTERIZATION OF FIII/YY1, A XENOPUS-LAEVIS CONSERVED ZINC-FINGER PROTEIN-BINDING TO THE FIRST EXON OF L1 AND L14 RIBOSOMAL-PROTEIN GENES

被引：37

作者：

PISANESCHI, G ^{[1
]}

CECCOTTI, S ^{[1
]}

FALCHETTI, ML ^{[1
]}

FIUMICINO, S ^{[1
]}

CARNEVALI, F ^{[1
]}

BECCARI, E ^{[1
]}

机构：

[1] UNIV ROMA LA SAPIENZA,CNR,CTR STUDIO GLI ACIDI NUCL,DIPARTIMENTO GENET & BIOL MOLEC,I-00185 ROME,ITALY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 205卷 / 02期

关键词：

D O I：

10.1006/bbrc.1994.2797

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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) LI and L14. (C) 1994 Academic Press, Inc.

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页码：1236 / 1242

页数：7

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