A FINGER PROTEIN STRUCTURALLY SIMILAR TO TFIIIA THAT BINDS EXCLUSIVELY TO 5S RNA IN XENOPUS

被引：102

作者：

JOHO, KE

DARBY, MK

CRAWFORD, ET

BROWN, DD

机构：

[1] Department of Embryology Carnegie Institution of Washington, Baltimore, MD 21210

来源：

CELL | 1990年 / 61卷 / 02期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0092-8674(90)90809-S

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：

A 5S RNA binding protein (p43) in Xenopus is a major constituent of oocytes and comprises part of a 42S ribonucleoprotein storage particle. We have cloned and sequenced p43 cDNA from X. laevis and X. borealis as well as the cDNA for X. borealis TFIIIA. Like TFIIIA, p43 has nine zinc fingers, seven of which are exactly the same size as their counterparts in TFIIIA. Amino acid homology between the two proteins is restricted mainly to conserved residues characteristic of zinc fingers. In contrast to TFIIIA, which binds specifically to both 5S RNA and 5S RNA genes, p43 binds exclusively to 5S RNA. © 1990.

引用

页码：293 / 300

页数：8

共 29 条

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