Premium
The processing of a Benzo(a)pyrene adduct into a frameshift or a base substitution mutation requires a different set of genes in Escherichia coli
Author(s) -
LenneSamuel Nathalie,
JanelBintz Regine,
Kolbanovskiy Aleksandr,
Geacintov Nicholas E.,
Fuchs Robert P. P.
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.02116.x
Subject(s) - biology , frameshift mutation , escherichia coli , substitution (logic) , genetics , mutation , base (topology) , gene , adduct , pyrene , microbiology and biotechnology , chemistry , computer science , programming language , mathematical analysis , mathematics , organic chemistry , astrobiology
Replication through a single DNA lesion may give rise to a panel of translesion synthesis (TLS) events, which comprise error‐free TLS, base substitutions and frameshift mutations. In order to determine the genetic control of the various TLS events induced by a single lesion, we have chosen the major N2‐dG adduct of (+)‐ anti ‐Benzo(a)pyrene diol epoxide [(+)‐ anti ‐BPDE] adduct located within a short run of guanines as a model lesion. Within this sequence context, in addition to the major event, i.e. error‐free TLS, the adduct also induces base substitutions (mostly G → T transversions) and −1 frameshift mutations. The pathway leading to G → T base substitution mutagenesis appears to be SOS independent, suggesting that TLS is most probably performed by the replicative Pol III holoenzyme itself. In contrast, both error‐free and frameshift TLS pathways are dependent upon SOS‐encoded functions that belong to the pool of inducible DNA polymerases specialized in TLS (translesional DNA polymerases), namely umuDC (Pol V) and dinB (Pol IV). It is likely that, given the diversity of conformations that can be adopted by lesion‐containing replication intermediates, cells use one or several translesional DNA polymerases to achieve TLS.