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Cited by 361RNA Research and SplicingRNA and protein synthesis mechanismsBiochemical and Molecular Research

Glyceraldehyde-3-phosphate Dehydrogenase Selectively Binds AU-rich RNA in the NAD+-binding Region (Rossmann Fold)

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Nagy, Eszter, Rigby, William F.C.·1995·Journal of Biological Chemistry
DOI 10.1074/jbc.270.6.2755
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Abstract

A 36-kDa protein that binds AU-rich RNA was purified from human spleen and identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). GAPDH has been previously demonstrated to bind tRNA with high affinity. Competition studies suggested that cytoplasmic GAPDH binds the AU-rich elements (AREs) of lymphokine mRNA 3'-untranslated regions with higher affinity than tRNA. The AUUUA-specific RNA binding activity of GAPDH was inhibited by NAD+, NADH, and ATP in a concentration-dependent manner, suggesting that RNA binding of GAPDH might involve the NAD(+)-binding region, or dinucleotide-binding (Rossmann) fold. This hypothesis was supported by experiments that localized RNA binding to the predicted N-terminal 6.8-kDa peptide, known to be involved in the formation of the NAD(+)-binding domain. The direct demonstration of ARE-specific binding protein activity localized to the NAD(+)-binding region of GAPDH supports the general concept that enzymes containing this domain may exhibit specific RNA binding activity and play additional roles in nucleic acid metabolism. Finally, cytoplasmic GAPDH was found in the polysomal fraction of T lymphocytes. Thus, the RNA binding specificity of GAPDH as well as its localization within the cell merit its strong consideration as a protein important in the regulation of ARE-dependent mRNA turnover and translation in addition to its well described role in glycolysis.

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  • GAPDH is a multifunctional enzyme that can bind a range of RNAs, including AU-rich regions in the 3' untranslated region (UTR) of cytokine mRNAs, including IFN-γ and IL-2.

    “GAPDH is a multifunctional enzyme that can bind a range of RNAs, including AU-rich regions in the 3’ untranslated region (UTR) of cytokine mRNAs, including IFN-γ and IL-2 (111).”

    From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [111]

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Authors
Nagy, E., & Rigby, W. F. C.
Affiliations
White River Junction VA Medical Center (US)
Corresponding author
Rigby, William F.C.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1995-02
Volume
270
Issue
6
Pages
2755-2763
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.270.6.2755
OpenAlex
W2050843429
Cited by
361
References
67
Citations by year
2026: 5 · 2025: 14 · 2024: 10 · 2023: 7 · 2022: 5 · 2021: 4 · 2020: 18 · 2019: 9 · 2018: 15 · 2017: 10 · 2016: 12 · 2015: 7 · 2014: 12 · 2013: 11 · 2012: 14
FWCI
6.32
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5k04ai000910-02)
  • National Institute of Allergy and Infectious Diseases (KO4 AI00910, R0 1 AI2434)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords
glyceraldehyde-3-phosphate dehydrogenase, NAD-binding domain, Rossmann fold, RNA-binding proteins, tRNA binding, 3' untranslated region, mRNA turnover, translational regulation, T cells, polysomes
MeSH terms
Adenine, Base Sequence, Cells, Cultured, Glyceraldehyde-3-Phosphate Dehydrogenases, Humans, Molecular Sequence Data, NAD, Protein Binding, RNA, Substrate Specificity, T-Lymphocytes, Uridine, Protein Folding

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