Dehydrogenases from all three domains of life cleave RNA.
Specific interactions of glyceraldehyde-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 degrees C, at MgCl(2) 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 of 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.
D019843:Archaeal Proteins / Q000378:metabolism*; D001483:Base Sequence; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D019642:RNA, Archaeal / Q000737:chemistry / Q000378:metabolism*; D016944:Sulfolobus / Q000201:enzymology
D019843:Archaeal Proteins; D019642:RNA, Archaeal; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases