The Escherichia coli protein YjjG is a house-cleaning nucleotidase in vivo
Article first published online: 5 FEB 2007
DOI: 10.1111/j.1574-6968.2007.00646.x
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How to Cite
Titz, B., Häuser, R., Engelbrecher, A. and Uetz, P. (2007), The Escherichia coli protein YjjG is a house-cleaning nucleotidase in vivo. FEMS Microbiology Letters, 270: 49–57. doi: 10.1111/j.1574-6968.2007.00646.x
Publication History
- Issue published online: 5 FEB 2007
- Article first published online: 5 FEB 2007
- Received 12 October 2006; revised 28 November 2006; accepted 5 January 2007.First published online 5 February 2007.
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Keywords:
- DNA repair;
- 5-fluorouracil;
- house-cleaning enzyme;
- bromodeoxyuridine;
- antimetabolites;
- drug metabolic detoxication
Abstract
House-cleaning enzymes protect cells from the adverse effects of noncanonical metabolic chemical compounds. The Escherichia coli nucleotide phosphatase YjjG (B4374, JW4336) functions as a house-cleaning phosphatase in vivo. YjjG protects the cell against noncanonical pyrimidine derivatives such as 5-fluoro-2′-deoxyuridine (5-FdUridine), 5-fluorouridine, 5-fluoroorotic acid (5-FOA), 5-fluorouracil, and 5-aza-2′-deoxycytidine. YjjG prevents the incorporation of potentially mutagenic nucleotides into DNA as shown for 5-bromo-2′-deoxyuridine (BrdU). Its enzymatic activity in vitro towards noncanonical 5-fluoro-2′-deoxyuridine monophosphate (5-FdUMP) is higher than towards canonical thymidine monophosphate (dTMP). The closest homolog in humans, HDHD4, does not show a protective effect against noncanonical nucleotides, excluding an involvement of HDHD4 in resistance against noncanonical nucleotides used for cancer chemotherapy. The substrate spectrum of YjjG suggests that its in vivo substrates are noncanonical pyrimidine derivatives, which might also include oxidized nucleobases such as 5-formyluracil and 5-hydroxyuracil.

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