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A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA
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| Zeitschriftentitel: | Genes & Development |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Genes & Development, 15, 2001, 4, S. 415-427 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
|
| Schlagwörter: |
| author_facet |
Voloshin, Oleg N. Ramirez, Benjamin E. Bax, Ad Camerini-Otero, R. Daniel Voloshin, Oleg N. Ramirez, Benjamin E. Bax, Ad Camerini-Otero, R. Daniel |
|---|---|
| author |
Voloshin, Oleg N. Ramirez, Benjamin E. Bax, Ad Camerini-Otero, R. Daniel |
| spellingShingle |
Voloshin, Oleg N. Ramirez, Benjamin E. Bax, Ad Camerini-Otero, R. Daniel Genes & Development A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA Developmental Biology Genetics |
| author_sort |
voloshin, oleg n. |
| spelling |
Voloshin, Oleg N. Ramirez, Benjamin E. Bax, Ad Camerini-Otero, R. Daniel 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.862901 <jats:p>DinI is a recently described negative regulator of the SOS response in <jats:italic>Escherichia coli</jats:italic>. Here we show that it physically interacts with RecA and prevents the binding of single-stranded DNA to RecA, which is required for the activation of the latter. DinI also displaces ssDNA from a stable RecA–DNA cofilament, thus eliminating the SOS signal. In addition, DinI inhibits RecA-mediated homologous DNA pairing, but has no effect on actively proceeding strand exchange. Biochemical data, together with the molecular structure, define the C-terminal α-helix in DinI as the active site of the protein. In an unusual example of molecular mimicry, a negatively charged surface on this α-helix, by imitating single-stranded DNA, interacts with the loop L2 homologous pairing region of RecA and interferes with the activation of RecA.</jats:p> A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA Genes & Development |
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| title |
A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_unstemmed |
A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_full |
A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_fullStr |
A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_full_unstemmed |
A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_short |
A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_sort |
a model for the abrogation of the sos response by an sos protein: a negatively charged helix in dini mimics dna in its interaction with reca |
| topic |
Developmental Biology Genetics |
| url |
http://dx.doi.org/10.1101/gad.862901 |
| publishDate |
2001 |
| physical |
415-427 |
| description |
<jats:p>DinI is a recently described negative regulator of the SOS response in <jats:italic>Escherichia coli</jats:italic>. Here we show that it physically interacts with RecA and prevents the binding of single-stranded DNA to RecA, which is required for the activation of the latter. DinI also displaces ssDNA from a stable RecA–DNA cofilament, thus eliminating the SOS signal. In addition, DinI inhibits RecA-mediated homologous DNA pairing, but has no effect on actively proceeding strand exchange. Biochemical data, together with the molecular structure, define the C-terminal α-helix in DinI as the active site of the protein. In an unusual example of molecular mimicry, a negatively charged surface on this α-helix, by imitating single-stranded DNA, interacts with the loop L2 homologous pairing region of RecA and interferes with the activation of RecA.</jats:p> |
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| author | Voloshin, Oleg N., Ramirez, Benjamin E., Bax, Ad, Camerini-Otero, R. Daniel |
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| description | <jats:p>DinI is a recently described negative regulator of the SOS response in <jats:italic>Escherichia coli</jats:italic>. Here we show that it physically interacts with RecA and prevents the binding of single-stranded DNA to RecA, which is required for the activation of the latter. DinI also displaces ssDNA from a stable RecA–DNA cofilament, thus eliminating the SOS signal. In addition, DinI inhibits RecA-mediated homologous DNA pairing, but has no effect on actively proceeding strand exchange. Biochemical data, together with the molecular structure, define the C-terminal α-helix in DinI as the active site of the protein. In an unusual example of molecular mimicry, a negatively charged surface on this α-helix, by imitating single-stranded DNA, interacts with the loop L2 homologous pairing region of RecA and interferes with the activation of RecA.</jats:p> |
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| imprint | Cold Spring Harbor Laboratory, 2001 |
| imprint_str_mv | Cold Spring Harbor Laboratory, 2001 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 415-427 |
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| spelling | Voloshin, Oleg N. Ramirez, Benjamin E. Bax, Ad Camerini-Otero, R. Daniel 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.862901 <jats:p>DinI is a recently described negative regulator of the SOS response in <jats:italic>Escherichia coli</jats:italic>. Here we show that it physically interacts with RecA and prevents the binding of single-stranded DNA to RecA, which is required for the activation of the latter. DinI also displaces ssDNA from a stable RecA–DNA cofilament, thus eliminating the SOS signal. In addition, DinI inhibits RecA-mediated homologous DNA pairing, but has no effect on actively proceeding strand exchange. Biochemical data, together with the molecular structure, define the C-terminal α-helix in DinI as the active site of the protein. In an unusual example of molecular mimicry, a negatively charged surface on this α-helix, by imitating single-stranded DNA, interacts with the loop L2 homologous pairing region of RecA and interferes with the activation of RecA.</jats:p> A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA Genes & Development |
| spellingShingle | Voloshin, Oleg N., Ramirez, Benjamin E., Bax, Ad, Camerini-Otero, R. Daniel, Genes & Development, A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA, Developmental Biology, Genetics |
| title | A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_full | A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_fullStr | A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_full_unstemmed | A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_short | A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| title_sort | a model for the abrogation of the sos response by an sos protein: a negatively charged helix in dini mimics dna in its interaction with reca |
| title_unstemmed | A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA |
| topic | Developmental Biology, Genetics |
| url | http://dx.doi.org/10.1101/gad.862901 |