Blocking the RecA activity and SOS-response in bacteria with a short α-helical peptide. Yakimov, A., Pobegalov, G., Bakhlanova, I., Khodorkovskii, M., Petukhov, M., & Baitin, D. Nucleic Acids Research, 45(16):9788-9796, Oxford University Press, 2017. cited By 5![Blocking the RecA activity and SOS-response in bacteria with a short α-helical peptide [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The RecX protein, a very active natural RecA protein inhibitor, can completely disassemble RecA filaments at nanomolar concentrations that are two to three orders of magnitude lower than that of RecA protein. Based on the structure of RecX protein complex with the presynaptic RecA filament, we designed a short first in class α-helical peptide that both inhibits RecA protein activities in vitro and blocks the bacterial SOS-response in vivo. The peptide was designed using SEQOPT, a novel method for global sequence optimization of protein α-helices. SEQOPT produces artificial peptide sequences containing only 20 natural amino acids with the maximum possible conformational stability at a given pH, ionic strength, temperature, peptide solubility. It also accounts for restrictions due to known amino acid residues involved in stabilization of protein complexes under consideration. The results indicate that a few key intermolecular interactions inside the RecA protein presynaptic complex are enough to reproduce the main features of the RecX protein mechanism of action. Since the SOS-response provides a major mechanism of bacterial adaptation to antibiotics, these results open new ways for the development of antibiotic co-therapy that would not cause bacterial resistance. © The Author(s) 2017.
@ARTICLE{Yakimov20179788,
author={Yakimov, A. and Pobegalov, G. and Bakhlanova, I. and Khodorkovskii, M. and Petukhov, M. and Baitin, D.},
title={Blocking the RecA activity and SOS-response in bacteria with a short α-helical peptide},
journal={Nucleic Acids Research},
year={2017},
volume={45},
number={16},
pages={9788-9796},
doi={10.1093/nar/gkx687},
note={cited By 5},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85031894382&doi=10.1093%2fnar%2fgkx687&partnerID=40&md5=7c23734641d4dc586d4b273bd6883cd5},
affiliation={Department of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, B.P.Konstantinov of National Research Centre Kurchatov Institute, Gatchina, 188300, Russian Federation; Peter the Great St Petersburg Polytechnic University, St-Petersburg, 195251, Russian Federation},
abstract={The RecX protein, a very active natural RecA protein inhibitor, can completely disassemble RecA filaments at nanomolar concentrations that are two to three orders of magnitude lower than that of RecA protein. Based on the structure of RecX protein complex with the presynaptic RecA filament, we designed a short first in class α-helical peptide that both inhibits RecA protein activities in vitro and blocks the bacterial SOS-response in vivo. The peptide was designed using SEQOPT, a novel method for global sequence optimization of protein α-helices. SEQOPT produces artificial peptide sequences containing only 20 natural amino acids with the maximum possible conformational stability at a given pH, ionic strength, temperature, peptide solubility. It also accounts for restrictions due to known amino acid residues involved in stabilization of protein complexes under consideration. The results indicate that a few key intermolecular interactions inside the RecA protein presynaptic complex are enough to reproduce the main features of the RecX protein mechanism of action. Since the SOS-response provides a major mechanism of bacterial adaptation to antibiotics, these results open new ways for the development of antibiotic co-therapy that would not cause bacterial resistance. © The Author(s) 2017.},
correspondence_address1={Baitin, D.; Department of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, B.P.Konstantinov of National Research Centre Kurchatov InstituteRussian Federation; email: dimabaitin@yahoo.com},
publisher={Oxford University Press},
issn={03051048},
coden={NARHA},
pubmed_id={28934502},
language={English},
abbrev_source_title={Nucleic Acids Res.},
document_type={Article},
source={Scopus},
}
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