Download Nucleotide sequence of the Streptococcus pneumoniae ung gene

Nucleic Acids Research, Vol. 18, No. 22 6693
Nucleotide sequence of the Streptococcus pneumoniae
ung gene encoding uracil-DNA glycosylase
V.MeJean, I.Rives and J.-P.CIaverys*
Centre de Recherche de Biochimie et de GeYietique Cellulaires du CNRS, 118 route de Narbonne,
31062 Toulouse Cedex, France
Submitted October 16, 1990
EMBL accession no. X55651
conservation of uracil-DNA glycosylases are witnesses of a
biologically significant direct role in mutation avoidance.
Uracil-DNA glycosylase, the enzyme responsible for the removal
of uracil from DNA (1), is directly involved in mutation
avoidance (2). Indeed, it is likely to prevent transition mutations
by removing uracil that results from deamination of cytosine.
It has been proposed that the removal of misincorporated uracil
by uracil-DNA glycosylase also plays an indirect role in
correction of replication errors in nascent strands (3): single
stranded gaps resulting from the removal of uracil might target
the generalized mismatch repair system of Streptococcus
pneumoniae (4) to nascent strands.
With the aim of investigating the role of uracil-DNA
glycosylase, we generated a ung~ mutant and characterized the
ung gene of 5. pneumoniae. We report its nucleotide sequence
here (fig. 1). The enzyme appears highly conserved from human
to Gram" (Escherichia coif) (5) and to Gram+ (5. pneumoniae)
bacteria (fig. 2). Investigation of mutation rates offers no support
to the hypothesis of a role of the enzyme in targeting generalized
mismatch repair (V.M., J.-C. Dev&Ijian, I.R., G. Alloing and
J.-P.C, in preparation). Nevertheless, the ubiquity and
ACKNOWLEDGEMENT
This work was supported by grants from the Association pour
la Recherche sur le Cancer.
REFERENCES
1. Lindahl.T. (1982) Annu. Rev. Biochem. 51, 61-87.
2. Duncan.B.K. and Weiss.B. (1982) J. Baaeriol. 151, 750-755.
3. Claverys.J.P., Roger.M. and Sicard.A.M. (1980) Mot. Gen. Genet. 178,
191-201.
4. Claverys.J.P. and Lacks,S.A. (1986) Microbiol. Rev. 50, 133-165.
5. Olsen.L.C, Aasland.R., Wittwer.C.U., Krokan.H.E. and Helland.D.E.
(1989) EMBOJ. 8, 3121-3125.
6. Varshney.U., HutcheonJ. and Van de SandcJ.H. (1988) J. Biol. Chem.
263, 7776-7784.
1 TTT CCT ATA ATA C M OCA OTA AAA ATS A M CAP TCC. OCT ATS. GAA CAC TCC TCT TGO CAT GCT TTO A n A M PCS
88 GOT TAT n C COG A M ATC AAT C M TTT ATG C M C M QTC TAT TCT C M CCQ A n A n TAT CCA CCC A M CAA AM
173 CTC TTO ACA ACA CTO CTT OAA OAA OTT A M OTC OTA ATT CTA OSS CAA OAC CCC TAT CAC OCA CCA OCT CAA CCS
262 TTT TCT OTA CCT OAC TCT ATC CCA CCT CCA CCA TCC TTC CAA AAT ATC TTS AAA OAA n o TCA CAT GAT ATC OOA
3*9
*3*
523
610
CAT
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GSA
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Tn
m
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AM
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m
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CTT m CM GCT
CAC CCC I T S UT
On AAS AAA TCT
CCC AAT GST CAT OCT
OTA CTC TOG CCA CCT
TTO TCO OTT TAT AOA
TCC C n AOA TAA
Figure 1. Nucleotide sequence of S. pneumoniae ung gene. Potential Shine- Dalgarno sequence, start and stop sites are underlined.
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Figure 2. Amino acid comparison of S. pneumoniae, E. coli (6) and human (5) uracil-DNA glycosylases. The S. pneumoniae protein sequence (217 amino acid
residues) is 48.4% and 48.8% identical to the E. coli and human proteins, respectively. ( - ) denotes identical matches. (.) denotes gap in the sequence to optimize
the alignment.
* To whom correspondence should be addressed