| pubmed-article:10899995 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C0019247 | lld:lifeskim |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C1509144 | lld:lifeskim |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:10899995 | lifeskim:mentions | umls-concept:C0337051 | lld:lifeskim |
| pubmed-article:10899995 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:10899995 | pubmed:dateCreated | 2000-8-24 | lld:pubmed |
| pubmed-article:10899995 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10899995 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10899995 | pubmed:abstractText | Three cytosolic and one plasma membrane-bound 5'-nucleotidases have been cloned and characterized. Their various substrate specificities suggest widely different functions in nucleotide metabolism. We now describe a 5'-nucleotidase in mitochondria. The enzyme, named dNT-2, dephosphorylates specifically the 5'- and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides. The cDNA of human dNT-2 codes for a 25.9-kDa polypeptide with a typical mitochondrial leader peptide, providing the structural basis for two-step processing during import into the mitochondrial matrix. The deduced amino acid sequence is 52% identical to that of a recently described cytosolic deoxyribonucleotidase (dNT-1). The two enzymes share many catalytic properties, but dNT-2 shows a narrower substrate specificity. Mitochondrial localization of dNT-2 was demonstrated by the mitochondrial fluorescence of 293 cells expressing a dNT-2-green fluorescent protein (GFP) fusion protein. 293 cells expressing fusion proteins without leader peptide or with dNT-1 showed a cytosolic fluorescence. During in vitro import into mitochondria, the preprotein lost the leader peptide. We suggest that dNT-2 protects mitochondrial DNA replication from overproduction of dTTP, in particular in resting cells. Mitochondrial toxicity of dTTP can be inferred from a severe inborn error of metabolism in which the loss of thymidine phosphorylase led to dTTP accumulation and aberrant mitochondrial DNA replication. We localized the gene for dNT-2 on chromosome 17p11.2 in the Smith-Magenis syndrome-critical region, raising the possibility that dNT-2 is involved in the etiology of this genetic disease. | lld:pubmed |
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| pubmed-article:10899995 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10899995 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10899995 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10899995 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10899995 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10899995 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10899995 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10899995 | pubmed:author | pubmed-author:MilaneseAA | lld:pubmed |
| pubmed-article:10899995 | pubmed:author | pubmed-author:BianchiVV | lld:pubmed |
| pubmed-article:10899995 | pubmed:author | pubmed-author:ReichardPP | lld:pubmed |
| pubmed-article:10899995 | pubmed:author | pubmed-author:RampazzoCC | lld:pubmed |
| pubmed-article:10899995 | pubmed:author | pubmed-author:GallinaroLL | lld:pubmed |
| pubmed-article:10899995 | pubmed:author | pubmed-author:FrigimelicaEE | lld:pubmed |
| pubmed-article:10899995 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10899995 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:10899995 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:10899995 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10899995 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10899995 | pubmed:pagination | 8239-44 | lld:pubmed |
| pubmed-article:10899995 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:10899995 | pubmed:meshHeading | pubmed-meshheading:10899995... | lld:pubmed |
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| pubmed-article:10899995 | pubmed:meshHeading | pubmed-meshheading:10899995... | lld:pubmed |
| pubmed-article:10899995 | pubmed:meshHeading | pubmed-meshheading:10899995... | lld:pubmed |
| pubmed-article:10899995 | pubmed:meshHeading | pubmed-meshheading:10899995... | lld:pubmed |
| pubmed-article:10899995 | pubmed:meshHeading | pubmed-meshheading:10899995... | lld:pubmed |
| pubmed-article:10899995 | pubmed:meshHeading | pubmed-meshheading:10899995... | lld:pubmed |
| pubmed-article:10899995 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10899995 | pubmed:articleTitle | A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. | lld:pubmed |
| pubmed-article:10899995 | pubmed:affiliation | Departments of Biology and Biomedical Sciences, University of Padua, I-35131 Padua, Italy. | lld:pubmed |
| pubmed-article:10899995 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10899995 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
