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Cited by 38RNA and protein synthesis mechanismsRNA Research and SplicingGenomics and Chromatin Dynamics

The 3‘ Untranslated Region of Manganese Superoxide Dismutase RNA Contains a Translational Enhancer Element

Chung, David J., Wright, Angelique E., Clerch, Linda Biadasz·1998·Biochemistry
DOI 10.1021/bi980935g
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Abstract

A redox-sensitive protein that binds to the 3' untranslated region (UTR) of manganese superoxide dismutase (MnSOD) RNA has been described previously [Fazzone, H., Wangner, A., and Clerch, L. B. (1993) J. Clin. Invest. 92, 1278-1281; Chung, D. J., and Clerch, L. B. (1997) Am. J. Physiol. 16, L714-L719]. In the present study, cross-competition gel retardation and RNase H assays were used to identify a 41-base region located 111 bases downstream of the stop codon as the 3' UTR cis element involved in protein binding. The base sequence of this region is approximately 75% conserved among the 3' UTRs of rat, mouse, cow, and human MnSOD mRNAs at approximately the same distance downstream of the stop codon. The role of this protein-binding region in RNA translation was assessed in an in vitro rabbit reticulocyte lysate system. Translation of MnSOD RNA from which the 3' UTR element was deleted decreased 60% compared with translation of MnSOD RNA containing the 3' UTR cis element. In the presence of a specific competitor oligoribonucleotide that inhibits MnSOD RNA protein-binding activity, translation of MnSOD RNA containing the 3' UTR was decreased by 65%. Thus, both the cis element and RNA protein-binding activity were required for more efficient translation of the MnSOD. An analysis of ribosomal profiles suggests the MnSOD RNA-binding protein participates in the formation of the translation initiation complex. When MnSOD RNA-binding activity was inhibited, initiation complex formation was decreased by 50%. From the data obtained in this study, we propose that the 3' UTR cis element of MnSOD through its interaction with MnSOD RNA-binding protein may function as a translational enhancer.

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Authors
Chung, D. J., Wright, A. E., & Clerch, L. B.
Affiliations
  • Georgetown University (US)
  • Lung Biology Laboratory, Departments of Physiology and Biophysics and Pediatrics, Georgetown University School of Medicine, Washington, D.C. 20007
ORCID
Chung, David J.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1998-10-26
Volume
37
Issue
46
Pages
16298-16306
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi980935g
OpenAlex
W2025645285
Semantic Scholar
1ca7c3bfa4d506c4aaa54351d7ff5a56348241ed
Cited by
38
References
12
Citations by year
2025: 1 · 2024: 1 · 2022: 2 · 2021: 1 · 2018: 2 · 2016: 1 · 2013: 1 · 2012: 4
FWCI
0.58
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Heart, Lung, and Blood Institute (HL 47413)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
manganese superoxide dismutase, 3' untranslated region, translational enhancer, RNA-binding proteins, cis-regulatory elements, translation initiation complex, redox-sensitive proteins, sequence conservation, reticulocyte lysate translation
MeSH terms
Animals, Base Sequence, Cattle, Cell Fractionation, Enhancer Elements, Genetic, Humans, Molecular Sequence Data, Peptide Chain Initiation, Translational, Peptide Mapping, Rabbits, Reticulocytes, RNA, Superoxide Dismutase, Protein Biosynthesis, RNA-Binding Proteins, Rats, Sprague-Dawley, 3' Untranslated Regions, Mice, Rats

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