Search | VHL Regional Portal

A finger protein structurally similar to TFIIIA that binds exclusively to 5S RNA in Xenopus.

Joho, K E; Darby, M K; Crawford, E T; Brown, D D.

Cell ; 61(2): 293-300, 1990 Apr 20.

Article in English | MEDLINE | ID: mdl-2331751

ABSTRACT

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.

Subject(s)

Carrier Proteins/genetics , Oocytes/metabolism , RNA, Ribosomal, 5S/metabolism , RNA, Ribosomal/metabolism , RNA-Binding Proteins , Ribosomal Proteins , Transcription Factors/genetics , Xenopus Proteins , Amino Acid Sequence , Animals , Blotting, Northern , Carrier Proteins/metabolism , Cloning, Molecular , DNA/genetics , DNA/metabolism , Female , Gene Library , Genes , Molecular Sequence Data , Protein Binding , RNA, Messenger/genetics , Ribonucleoproteins/biosynthesis , Ribonucleoproteins/isolation & purification , Sequence Homology, Nucleic Acid , Transcription Factor TFIIIA , Transcription Factors/metabolism , Xenopus laevis

ABSTRACT

Subject(s)

SEND TO:

SELECTION OF CITATIONS

SEARCH DETAIL