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Journal of Bacteriology, June 2000, p. 3353-3360, Vol. 182, No. 12
Laboratoire de Microbiologie et
Génétique Moléculaires, Université Paul
Sabatier, Toulouse, France
Received 6 December 1999/Accepted 16 March 2000
The unusual behavior of the mutation ami36, which
generates hyperrecombination in two point crosses, was previously
attributed to a localized conversion process changing A/G mispairs into
CG pairs. Although the mechanism was found to be dependent on the DNA
polymerase I, the specific function responsible for this correction was
still unknown. Analysis of the pneumococcal genome sequence has
revealed the presence of an open reading frame homologous to the gene
mutY of Escherichia coli. The gene
mutY encodes an adenine glycosylase active on A/G and
A/7,8-dihydro-8-oxoguanine (8-OxoG) mismatches, inducing their repair
to CG and C/8-OxoG, respectively. Here we report that disrupting the
pneumococcal mutY homologue abolishes the
hyperrecombination induced by ami36 and leads to a mutator
phenotype specifically enhancing AT-to-CG transversions. The deduced
amino acid sequence of the pneumococcal MutY protein reveals the
absence of four cysteines, highly conserved in the endonuclease
III/MutY glycosylase family, which ligate a [4Fe-4S]2+
cluster. The actual function of this cluster is still intriguing, inasmuch as we show that the pneumococcal gene complements a
mutY strain of E. coli.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Hyperrecombination in Streptococcus
pneumoniae Depends on an Atypical mutY
Homologue
and
*
Corresponding author. Mailing address: Laboratoire de
Microbiologie et Génétique Moléculaires du CNRS,
Université Paul Sabatier, 118 route de Narbonne, 31062 Toulouse
Cedex, France. Phone: 561-33-59-71. Fax: 561-33-58-86. E-mail:
pasta{at}ibcg.biotoul.fr.
Present address: Department of Veterinary and Biomedical Sciences,
Lincoln, NE 68503.
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