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Binding of the La autoantigen to the 5' untranslated region of a chimeric human translation elongation factor 1A reporter mRNA inhibits translation in vitro.
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- Author(s): Zhu J;Zhu J; Hayakawa A; Kakegawa T; Kaspar RL
- Source:
Biochimica et biophysica acta [Biochim Biophys Acta] 2001 Oct 31; Vol. 1521 (1-3), pp. 19-29.
- Publication Type:
Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
- Language:
English
- Additional Information
- Source:
Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE
- Publication Information:
Original Publication: Amsterdam : Elsevier Pub. Co.
- Subject Terms:
- Abstract:
Human translation elongation factor 1A (EF1A) is a member of a large class of mRNAs, including ribosomal proteins and other translation elongation factors, which are coordinately translationally regulated under various conditions. Each of these mRNAs contains a terminal oligopyrimidine tract (TOP) that is required for translational control. A human growth hormone (hGH) expression construct containing the promoter region and 5' untranslated region (UTR) of EF1A linked to the hGH coding region (EF1A/hGH) was translationally repressed following rapamycin treatment in similar fashion to endogenous EF1A in human B lymphocytes. Mutation of two nucleotides in the TOP motif abolished the translational regulation. Gel mobility shift assays showed that both La protein from human B lymphocyte cytoplasmic extracts as well as purified recombinant La protein specifically bind to an in vitro-synthesized RNA containing the 5' UTR of EF1A mRNA. Moreover, extracts prepared from rapamycin-treated cells showed increased binding activity to the EF1A 5' UTR RNA, which correlates with TOP mRNA translational repression. In an in vitro translation system, recombinant La dramatically decreased the expression of EF1A/hGH construct mRNA, but not mRNAs lacking an intact TOP element. These results indicate that TOP mRNA translation may be modulated through La binding to the TOP element.
- Grant Information:
GM57644 United States GM NIGMS NIH HHS
- Accession Number:
0 (5' Untranslated Regions)
0 (Autoantigens)
0 (Peptide Elongation Factor 1)
0 (RNA, Messenger)
0 (Recombinant Proteins)
0 (Ribonucleoproteins)
12629-01-5 (Human Growth Hormone)
W36ZG6FT64 (Sirolimus)
- Publication Date:
Date Created: 20011103 Date Completed: 20011218 Latest Revision: 20231213
- Publication Date:
20240829
- Accession Number:
10.1016/s0167-4781(01)00277-9
- Accession Number:
11690632
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