Journal article

Publication year: 2002

Pages: 46145-46150

Journal: Journal of Biological Chemistry

Volume number: 277

Issue number: 48

ISSN: 0021-9258

Open access status: Hybrid

DOI Link: https://doi.org/10.1074/jbc.M208717200

Publisher: Elsevier

Abstract: 
Specific interactions of glyceraldehy-de-3-phosphate dehydrogenase (GAPDH) with RNA have been reported both in vitro and in vivo. We show that eukaryotic and bacterial GAPDH and two proteins from. the hyperthermophilic archaeon Sulfolobus solfataricus, which are annotated as dehydrogenases, cleave RNA producing similar degradation patterns. RNA cleavage is most efficient at 60 degreesC, at MgCl2, concentrations up to 5 mm, and takes place between pyrimidine and adenosine. The RNase active center of the putative aspartate semialdehyde dehydrogenase from S. solfataricus is located within the N-terminal 73 amino acids, which comprise the first mononucleotide-binding site (if the predicted Rossmann fold. Thus, RNA cleavage has to be taken into account in the ongoing discussion of the possible biological function of RNA binding by dehydrogenases.

Harvard Citation style: Evguenieva-Hackenberg, E., Schiltz, E. and Klug, G. (2002) Dehydrogenases from all three domains of life cleave RNA, Journal of Biological Chemistry, 277(48), pp. 46145-46150. https://doi.org/10.1074/jbc.M208717200

APA Citation style: Evguenieva-Hackenberg, E., Schiltz, E., & Klug, G. (2002). Dehydrogenases from all three domains of life cleave RNA. Journal of Biological Chemistry. 277(48), 46145-46150. https://doi.org/10.1074/jbc.M208717200