Revealing biophysical properties of KfrA-type proteins as a novel class of cytoskeletal, coiled-coil plasmid-encoded proteins
| العنوان: | Revealing biophysical properties of KfrA-type proteins as a novel class of cytoskeletal, coiled-coil plasmid-encoded proteins |
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| المؤلفون: | E. Sitkiewicz, Stanislaw Dunin-Horkawicz, G. Goch, Maciej Jasiński, Ewa Lewicka, Jan Ludwiczak, B. Swiderska, Grazyna Jagura-Burdzy, Malgorzata Adamczyk, H. Nieznanska, Roza Szatkowska |
| المصدر: | BMC Microbiology, Vol 21, Iss 1, Pp 1-16 (2021) BMC Microbiology |
| بيانات النشر: | BMC, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | Microbiology (medical), Cell division, Transcription, Genetic, In silico, Stability functions, lcsh:QR1-502, Biology, Microbiology, lcsh:Microbiology, 03 medical and health sciences, chemistry.chemical_compound, Plasmid, Bacterial Proteins, Escherichia coli, Protein–DNA interaction, Computer Simulation, Cytoskeleton, 030304 developmental biology, Coiled coil, 0303 health sciences, Binding Sites, 030306 microbiology, DNA-protein interaction, Self-assembly, Cell biology, Coiled-coil proteins, DNA binding site, DNA-Binding Proteins, Cytoskeletal Proteins, chemistry, Conjugation, Genetic, Broad-host-range plasmids, Brownian motion, DNA, Plasmids, Research Article |
| الوصف: | Background DNA binding KfrA-type proteins of broad-host-range bacterial plasmids belonging to IncP-1 and IncU incompatibility groups are characterized by globular N-terminal head domains and long alpha-helical coiled-coil tails. They have been shown to act as transcriptional auto-regulators. Results This study was focused on two members of the growing family of KfrA-type proteins encoded by the broad-host-range plasmids, R751 of IncP-1β and RA3 of IncU groups. Comparative in vitro and in silico studies on KfrAR751 and KfrARA3 confirmed their similar biophysical properties despite low conservation of the amino acid sequences. They form a wide range of oligomeric forms in vitro and, in the presence of their cognate DNA binding sites, they polymerize into the higher order filaments visualized as “threads” by negative staining electron microscopy. The studies revealed also temperature-dependent changes in the coiled-coil segment of KfrA proteins that is involved in the stabilization of dimers required for DNA interactions. Conclusion KfrAR751 and KfrARA3 are structural homologues. We postulate that KfrA type proteins have moonlighting activity. They not only act as transcriptional auto-regulators but form cytoskeletal structures, which might facilitate plasmid DNA delivery and positioning in the cells before cell division, involving thermal energy. |
| اللغة: | English |
| تدمد: | 1471-2180 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd996d0ca2cc83aa3f9d5f04c30774db https://doaj.org/article/e6faf88eca5d492fb54099ffe750885a |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....bd996d0ca2cc83aa3f9d5f04c30774db |
| قاعدة البيانات: | OpenAIRE |
Find this article in full text from Springer Verlag. | تدمد: | 14712180 |
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