PMID- 17143579
OWN - NLM
STAT- MEDLINE
DCOM- 20070809
LR  - 20181113
IS  - 0167-4412 (Print)
IS  - 0167-4412 (Linking)
VI  - 63
IP  - 4
DP  - 2007 Mar
TI  - Functional characterization of a gene encoding a dual domain for uridine kinase 
      and uracil phosphoribosyltransferase in Arabidopsis thaliana.
PG  - 465-77
AB  - 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.
FAU - Islam, M Rafiqul
AU  - Islam MR
AD  - Department of Biological Sciences, Seoul National University, Seoul 151-742, 
      Republic of Korea.
FAU - Kim, Hoyeun
AU  - Kim H
FAU - Kang, Shin-Wook
AU  - Kang SW
FAU - Kim, Jung-Sup
AU  - Kim JS
FAU - Jeong, Young-Min
AU  - Jeong YM
FAU - Hwang, Hyun-Ju
AU  - Hwang HJ
FAU - Lee, So-Young
AU  - Lee SY
FAU - Woo, Je-Chang
AU  - Woo JC
FAU - Kim, Sang-Gu
AU  - Kim SG
LA  - eng
SI  - GENBANK/AY089970
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Plant Mol Biol
JT  - Plant molecular biology
JID - 9106343
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Plant)
RN  - EC 2.4.2.- (Pentosyltransferases)
RN  - EC 2.4.2.9 (uracil phosphoribosyltransferase)
RN  - EC 2.7.1.48 (Uridine Kinase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Arabidopsis/*enzymology/*genetics
MH  - Arabidopsis Proteins/genetics
MH  - Base Sequence
MH  - DNA Primers
MH  - DNA, Plant/genetics
MH  - Escherichia coli/genetics
MH  - Expressed Sequence Tags
MH  - Genes, Reporter
MH  - Molecular Sequence Data
MH  - Pentosyltransferases/*genetics
MH  - Sequence Alignment
MH  - Transfection
MH  - Uridine Kinase/*genetics
EDAT- 2006/12/05 09:00
MHDA- 2007/08/10 09:00
CRDT- 2006/12/05 09:00
PHST- 2006/06/18 00:00 [received]
PHST- 2006/10/16 00:00 [accepted]
PHST- 2006/12/05 09:00 [pubmed]
PHST- 2007/08/10 09:00 [medline]
PHST- 2006/12/05 09:00 [entrez]
AID - 10.1007/s11103-006-9101-3 [doi]
PST - ppublish
SO  - Plant Mol Biol. 2007 Mar;63(4):465-77. doi: 10.1007/s11103-006-9101-3.