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
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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收藏
页码:1236 / 1242
页数:7
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