Correction: Insight into Molecular and Functional Properties of NMNAT3 Reveals New Hints of NAD Homeostasis within Human Mitochondria

• DOI: 10.1371/annotation/f5e6107f-a911-4c15-a881-7cb7e4946ff6
• Publication Date: 2013-12-11T16:38:19Z
• Authors: Roberta Felici; Andrea Lapucci; Matteo Ramazzotti; Alberto Chiarugi
• Keywords: Homeostasis

Among the enzymes involved in NAD homeostasis, nicotinamide mononucleotide adenylyltransferases (NMNAT1-3) are central to intracellular formation.Although NMNAT3 is postulated be a mitochondrial enzyme contributing NADdependent organelle functioning, information on endogenous proteins lacking.We report that human cells single gene nmnat3 localized chromosome 3 codes for two mRNA splice variants NMNATv1 and FKSG76, whereas previously reported NMNAT3v2 transcript not present.However, NMNAT3v1 FKSG76 detectable, consistent with finding an upstream ORF their mRNAs negatively regulates translation.NMNAT3v1 transfection demonstrates protein cytosolic inactive, but operates cleavage rather than synthesis.In keeping lack of NMNAT3, we show extracellular NAD, its metabolic precursors, sustains pool ATP-independent manner.Data present study modify scenario origin by showing that, cells, absent mitochondria, and, akin plants yeast, maintains pool.