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PMID: 8035819 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The cytoplasm of Xenopus oocytes contains a factor that protects double-stranded RNA from adenosine-to-inosine modification.

Molecular and cellular biology ·Vol. 14 ·No. 8 ·1994-08-00 ·Pages 5425-32

Saccomanno L, Bass BL

Abstract

Here we describe studies of double-stranded RNA (dsRNA) adenosine deaminase in Xenopus laevis, in particular during meiotic maturation, the period during which a stage VI oocyte matures to an egg. We show that dsRNA adenosine deaminase is in the nuclei of stage VI oocytes. Most importantly, we demonstrate that the cytoplasm of stage VI oocytes contains a factor that protects microinjected dsRNA from deamination when dsRNA adenosine deaminase is released from the nucleus during meiotic maturation. Our data suggest that the protection factor is a cytoplasmic dsRNA-binding protein or proteins that bind to dsRNA in a sequence-independent manner to occlude dsRNA from binding to dsRNA adenosine deaminase. The cytoplasmic double-stranded RNA-binding protein(s) does not bind to other nucleic acids and can be titrated at high concentrations of dsRNA. These studies raise the question of whether all dsRNA-binding proteins share endogenous substrates and also suggest potential means of regulating dsRNA adenosine deaminase in vivo.

MeSH Terms
Adenosine Deaminase/metabolism Adenosine Deaminase Inhibitors Animals Cell Nucleus/metabolism Cytoplasm/metabolism Female Meiosis Oocytes/metabolism RNA, Double-Stranded/metabolism RNA-Binding Proteins/metabolism Xenopus laevis
Chemicals
Adenosine Deaminase Inhibitors RNA, Double-Stranded RNA-Binding Proteins ADARB1 protein, human Adenosine Deaminase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Saccomanno L
Department of Biochemistry, University of Utah, Salt Lake City 84132.
Bass B L
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1994-08-00
Pages
5425-32
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC359061
Subset
IM
Grants
NIGMS NIH HHS · GM44073 · United States
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