Download Nucleotide sequence of the Streptococcus

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.Claverys*
Centre de Recherche de Biochimie et de Genetique Cellulaires du CNRS, 118 route de Narbonne,
31062 Toulouse Cedex, France
EMBL accession no. X55651
Submitted October 16, 1990
conservation of uracil-DNA glycosylases are witnesses of
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 S. pneumoniae. We report its nucleotide sequence
here (fig. 1). The enzyme appears highly conserved from human
to Gram- (Escherichia coli) (5) and to Gram+ (S. 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. Dev6djian, I.R., G. Alloing and
J.-P.C., in preparation). Nevertheless, the ubiquity and
1 TTT OCT
GGT TAT
CTC TTG
TTT TCT
CAT GAT
GGT CAA
TAT GCA
GG TTT
88
175
262
349
436
523
610
ATA ATA GAG OCA OTA
TTC GG0 AAA ATC MT
ACA ACA CTG CTT MA
GTA CCT GAC TCT ATC
TTG ACA GCT TOO OCT
ATC TOG GAG CCT TTT
CGT MG MG MG GCC
TGG GGT TCC AM CCT
AM ATG AMG
CAG TTT ATG
GM GTT AAM
CCA OCT CCA
GAG
ACT
TTA
TTT
CM
GAT
GTT
TCC
ACKNOWLEDGEMENT
This work was supported by grants from the Association
la Recherche sur le Cancer.
TTG
ATT
CCT
MT
CTT
CAG
CAT
ACA
1. Lindahl,T. (1982) Annu. Rev. Biochem. 51, 61-87.
2. Duncan,B.K. and Weiss,B. (1982) J. Bacteriol. 151, 750-755.
3. Claverys,J.P., Roger,M. and Sicard,A.M. (1980) Mol. 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) EMBO J. 8, 3121-3125.
6. Varshney,U., Hutcheon,T. and Van de Sande,J.H. (1988) J. Biol. Chem.
263, 7776-7784.
CTT
GTG
CAC
TTC
GM CAC
TCT CAG
G0G CM
MT ATC
MT OCT
GTC MT
TTG ATT
TTA AM
TCG TCT TOG CAT GCT TTG ATT MO GCG CM TTA CCT GAG
GG0 ATT ATT TAT CCA CCC MG MA MCG TT TTT CAG OCT
GAC CCC TAT
TTG AM GM
TGT TTG ACT
CAT CTA MAT
ATT GM TCA
GAG ACA GM
CAC GGA CCA GOT
TTG TCA MAT MAT
OTT CCT GCT GGA
AG CCA GTC GTT
GCC CAT CCA AGT
CM GAG CCA ATC
Figure 1. Nucleotide sequence of S. pneumoniae ung gene. Potential Shine- Dalgarno sequence,
(S. pneu.)
(E. cot!)
CHumn)
pour
REFERENCES
GA TCG GCT ATG
GAG CAG GTC TAT
GTG GTA ATT CTA
CCA TCC TTG CAA
GG GTC
GCT GTG
ACC MT
AMG GCC
a
CM GCG CAG
GMA GTT
0CC MT
GTA CTC
TTG TCG
CAT TOG CTT
ATC
CAG
TTT
CCT
GGC TTG AGT
MG AM TCT
GOT
TOG
GTT
ACA
CAT OCT
GMG CT
TAT AGA
TM
start and stop sites are underlined.
NEHS.SWNALIKAOLPEGTFGK. INOFNEOVYSGI ITPPKEKVFQALLTTLLEEVKVVILGGPTHGPGMAQGLSFSVPDSIPAPPSLONILKELSDDIGV. .KK
-ANELT--DVLAEEKOOP--LNTLOTVASERO-GVT --- -QKD--N-FRF-E-GD ----------------- N--A--- RPG-Al ---- L-MY--T- ENT-PGFTRP
ARNVPVGFGES-KKH-SG-FGK --- IK.-NOFVA-ERKHT-V ---PHO--TWTICD IK--------------- N -----C---ORPVPP ----E-1 ---- STD-ED-VH-
SHD.LTAUAEOGvLLLACLTVPAGHNAGoIWEpFTDAVIOVVWHLDRPVFVLWGAYARKKKALvTpHNLI IEMPSPLSVYRGFWGSKPFSKANTFLKETGOEPIDWLR
1-GY-ES--R -T-----TV---R----HS--SLG--T ---K--SLI-OHREG---L--- SH-0--G-IIDKOR-HVLKAP-A----AH --- F-CNH-VL--GW-EOR-ET ---- -PVLPA
G--D-SG- ------- A------H--N--KER- --0--A-V-WL--NSN-L ------- T----- SA--RK -----OTA------ VY ------ R--SKT-EL-GKS-KK----KEL
Figure 2. Amino acid comparison of S. pneumoniae, E. coli (6) and human (5) uracil-DNA glycosylases. The S. pneumoniae protein sequence (217 amnino 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