Bacteriophage GIL01 gp7 interacts with host LexA repressor to enhance DNA binding and inhibit RecA-mediated auto-cleavage
Fornelos Martins, N., Butala, M., Hodnik, V., Anderluh, G., Bamford, J., & Salas, M. (2015). Bacteriophage GIL01 gp7 interacts with host LexA repressor to enhance DNA binding and inhibit RecA-mediated auto-cleavage. Nucleic Acids Research, 43 (15), 7315-7329. doi:10.1093/nar/gkv634
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Nucleic Acids ResearchAuthors
Date
2015Discipline
Solu- ja molekyylibiologiaCopyright
© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License.
The SOS response in Eubacteria is a global response
to DNA damage and its activation is increasingly associated
with the movement of mobile genetic elements.
The temperate phage GIL01 is induced into
lytic growth using the host’s SOS response to genomic
stress. LexA, the SOS transcription factor, represses
bacteriophage transcription by binding to
a set of SOS boxes in the lysogenic promoter P1.
However, LexA is unable to efficiently repress GIL01
transcription unless the small phage-encoded protein
gp7 is also present. We found that gp7 forms a
stable complex with LexA that enhances LexA binding
to phage and cellular SOS sites and interferes
with RecA-mediated auto-cleavage of LexA, the key
step in the initiation of the SOS response. Gp7 did
not bind DNA, alone or when complexed with LexA.
Our findings suggest that gp7 induces a LexA conformation
that favors DNA binding but disfavors LexA
auto-cleavage, thereby altering the dynamics of the
cellular SOS response. This is the first account of an
accessory factor interacting with LexA to regulate
transcription.
...


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Except where otherwise noted, this item's license is described as © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License.
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