Source:http://linkedlifedata.com/resource/pubmed/id/17143579
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rdf:type | |
lifeskim:mentions |
umls-concept:C0042001,
umls-concept:C0077844,
umls-concept:C0079429,
umls-concept:C0162740,
umls-concept:C0205245,
umls-concept:C0679058,
umls-concept:C1514562,
umls-concept:C1547699,
umls-concept:C1554184,
umls-concept:C1880022,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2700640
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pubmed:issue |
4
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pubmed:dateCreated |
2007-6-5
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pubmed:databankReference | |
pubmed:abstractText |
Uridine kinase (UK) and uracil phosphoribosyltransferase (UPRT) are enzymes catalyzing the formation of uridine 5'-monophosphate (UMP) from uridine and adenine 5'-triphosphate (ATP) and from uracil and phosphoribosyl-alpha-l-pyrophosphate (PRPP), respectively, in the pyrimidine salvage pathway. Here, we report the characterization and functional analysis of a gene AtUK/UPRT1 from Arabidopsis thaliana. Sequencing of an expressed sequence tag clone of this gene revealed that it contains a full-length open reading frame of 1461 nucleotides and encodes a protein with a molecular mass of approximately 53 kDa. The sequence analysis revealed that the N-terminal region of AtUK/UPRT1 contains a UK domain and the C-terminal region consists of a UPRT domain. Expression of AtUK/UPRT1 in upp and upp-udk mutants of Escherichia coli supplied with 5-fluorouracil (5-FU) and 5-fluorouridine (5-FD) led to growth inhibition. Identical results were obtained with 5-FD and 5-FU treatments when the UK and UPRT domains were separated by the introduction of translation initiation and stop codons prior to complementation into the upp-udk and upp mutants. These results suggest that the AtUK/UPRT1 product can use uracil and uridine as substrates for the production of UMP. We also investigated the function of AtUK/UPRT1 in an Arabidopsis mutant. The wild-type Arabidopsis plants showed drastic growth retardation when they were treated with 5-FU and 5-FD while the growth of atuk/uprtl mutant plants was not significantly affected. These findings confirm that AtUK/UPRT1 has a dual role in coding for both uridine kinase and uracil phosphoribosyltransferase that form UMP through the pyrimidine salvage pathway in Arabidopsis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Pentosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/uracil phosphoribosyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0167-4412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
465-77
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pubmed:meshHeading |
pubmed-meshheading:17143579-Amino Acid Sequence,
pubmed-meshheading:17143579-Arabidopsis,
pubmed-meshheading:17143579-Arabidopsis Proteins,
pubmed-meshheading:17143579-Base Sequence,
pubmed-meshheading:17143579-DNA, Plant,
pubmed-meshheading:17143579-DNA Primers,
pubmed-meshheading:17143579-Escherichia coli,
pubmed-meshheading:17143579-Expressed Sequence Tags,
pubmed-meshheading:17143579-Genes, Reporter,
pubmed-meshheading:17143579-Molecular Sequence Data,
pubmed-meshheading:17143579-Pentosyltransferases,
pubmed-meshheading:17143579-Sequence Alignment,
pubmed-meshheading:17143579-Transfection,
pubmed-meshheading:17143579-Uridine Kinase
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pubmed:year |
2007
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pubmed:articleTitle |
Functional characterization of a gene encoding a dual domain for uridine kinase and uracil phosphoribosyltransferase in Arabidopsis thaliana.
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pubmed:affiliation |
Department of Biological Sciences, Seoul National University, Seoul 151-742, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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