Journal
NUCLEIC ACIDS RESEARCH
Volume 38, Issue 14, Pages 4834-4843Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkq249
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Funding
- The Ministry of Education, Culture, Sports, Science and Technology of Japan [20013034, 21117512]
- Japan Society for the Promotion of Science [19390114, 08J03650]
- Kyushu University
- Grants-in-Aid for Scientific Research [21117512, 08J03650, 20013034, 19390114] Funding Source: KAKEN
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Nucleotides function in a variety of biological reactions; however, they can undergo various chemical modifications. Such modified nucleotides may be toxic to cells if not eliminated from the nucleotide pools. We performed a screen for modified-nucleotide binding proteins and identified human nucleoside diphosphate linked moiety X-type motif 16 (NUDT16) protein as an inosine triphosphate (ITP)/xanthosine triphosphate (XTP)/GTP-binding protein. Recombinant NUDT16 hydrolyzes purine nucleoside diphosphates to the corresponding nucleoside monophosphates. Among 29 nucleotides examined, the highest k(cat)/K(m) values were for inosine diphosphate (IDP) and deoxyinosine diphosphate (dIDP). Moreover, NUDT16 moderately hydrolyzes (deoxy)inosine triphosphate ([d]ITP). NUDT16 is mostly localized in the nucleus, and especially in the nucleolus. Knockdown of NUDT16 in HeLa MR cells caused cell cycle arrest in S-phase, reduced cell proliferation, increased accumulation of single-strand breaks in nuclear DNA as well as increased levels of inosine in RNA. We thus concluded that NUDT16 is a (deoxy)inosine diphosphatase that may function mainly in the nucleus to protect cells from deleterious effects of (d)ITP.
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