Affiliation:
1. Department of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, The University of Vermont, Burlington, Vermont 05405-0068
Abstract
ABSTRACT
Escherichia coli
formamidopyrimidine (Fpg) DNA glycosylase and MutY DNA glycosylase are base excision repair proteins that work together to protect cells from the mutagenic effects of the commonly oxidized guanine product 7,8-dihydro-8-oxoguanine. The genes encoding these proteins,
fpg
and
mutY
, are both cotranscribed as part of complex operons.
fpg
is the terminal gene in an operon with the gene order
radC
,
rpmB
,
rpmG
, and
fpg
. This operon has transcription initiation sites upstream of
radC
, in the
radC
coding region, and immediately upstream of
fpg
. There is a strong attenuator in the
rpmG-fpg
intergenic region and three transcription termination sites downstream of
fpg
. There is an additional site, in the
radC-rpmB
intergenic region, that corresponds either to a transcription initiation site or to an RNase E or RNase III cleavage site.
mutY
is the first gene in an operon with the gene order
mutY
,
yggX
,
mltC
, and
nupG
. This operon has transcription initiation sites upstream of
mutY
, in the
mutY
coding region, and immediately upstream of
nupG
. There also appear to be attenuators in the
yggX-mltC
and
mltC-nupG
intergenic regions. The order of genes in these operons has been conserved or partially conserved only in other closely related gram-negative bacteria, although it is not known whether the genes are cotranscribed in these other organisms.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
16 articles.
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