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PMID: 3884610 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Membrane-bound mRNAs are recruited from preinitiated ribonucleoprotein particles in injected Xenopus oocytes.

The Journal of biological chemistry ·Vol. 260 ·No. 7 ·1985-04-10 ·Pages 4448-54

Richter JD, Lorenz LJ, Audet RG

Abstract

Messenger RNA injected Xenopus oocytes exhibit a differential capacity for translation. mRNAs translated in the free cytoplasm are translated efficiently whereas mRNAs translated on the rough endoplasmic reticulum (RER) membrane are translated inefficiently. If mRNA injected oocytes are injected additionally with proteins isolated from the RER, enhanced translation of RER-bound mRNAs is observed. When examined by sucrose gradient centrifugation and RNA dot blots, most of the injected RER-bound mRNA sediments less than or equal to the 80 S monosome. The RER proteins recruit these preinitiated mRNAs onto polysomes as evidenced by a shift in sedimentation to the polysome region of a sucrose gradient. When examined by immunoblotting, the RER proteins are shown to contain a protein which reacts specifically with an antibody directed against docking protein (SRP-receptor protein). However, this putative docking protein does not appear to be the protein which actually recruits the preinitiated mRNAs onto polysomes.

MeSH Terms
Animals Cytoplasm/metabolism Electrophoresis, Polyacrylamide Gel Endoplasmic Reticulum/metabolism Female Immunosorbent Techniques Microinjections Oocytes/metabolism Ovalbumin/biosynthesis Protein Biosynthesis RNA, Messenger/metabolism Ribonucleoproteins/metabolism Xenopus laevis
Chemicals
RNA, Messenger Ribonucleoproteins Ovalbumin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Richter J D
Lorenz L J
Audet R G
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1985-04-10
Pages
4448-54
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM34554 · United States
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