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Identification of the NAD+-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain

Lookup NU author(s): Professor Robert Lightowlers

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Abstract

There is growing evidence that metabolic enzymes may act as multifunctional proteins performing diverse roles in cellular metabolism. Among these functions are the RNA-binding activities of NAD+-dependent dehydrogenases. Previously, we have chartacterized the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an RNA-binding protein with preference to adenine-uracil-rich sequences. In this study, we used GST-GAPDH fusion proteins generated by deletion mutagenesis to search for the RNA binding domain. We established that the N-terminal 43 amino acid residues of GAPDH, which correspond to the first mononucleotide-binding domain of the NAD+-binding fold is sufficient to confer RNA-binding. We also provide evidence that this single domain, although it retains most of the RNA-binding activity, loses sequence specificity. Our results suggest a molecular basis for RNA-recognition by NAD+-dependent dehydrogenases and (di)nucleotide-binding metabolic enzymes that had been reported to have RNA-binding activity with different specificity. To support this prediction we also identified other members of the family of NAD+-dependent dehydrogenases with no previous history of nucleic acid binding as RNA binding proteins in vitro. Based on our findings we propose the addition of the NAD+-binding domain to the list of RNA binding domains/motifs. (C) 2000 Academic Press.


Publication metadata

Author(s): Lightowlers RN; Nagy E; Henics T; Eckert M; Miseta A; Kellermayer M

Publication type: Article

Publication status: Published

Journal: Biochemical and Biophysical Research Communications

Year: 2000

Volume: 275

Issue: 2

Pages: 253-260

ISSN (print): 0006-291X

ISSN (electronic): 1090-2104

Publisher: Academic Press

URL: http://dx.doi.org/10.1006/bbrc.2000.3246

DOI: 10.1006/bbrc.2000.3246

PubMed id: 10964654


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