Hauptseite > Publikationsdatenbank > The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding > print

001     903486
005     20240627202007.0
024 7 _ |a 10.1038/s41467-021-25429-2
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100 1 _ |a Parker, AV
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245 _ _ |a The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
260 _ _ |a [London]
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520 _ _ |a The efficient segregation of replicated genetic material is an essential step for cell division.Bacterial cells use several evolutionarily-distinct genome segregation systems, the mostcommon of which is the type I Par system. It consists of an adapter protein, ParB, that bindsto the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, thatbinds nonspecific DNA and mediates cargo transport. However, the molecular details of howthis system functions are not well understood. Here, we report the cryo-EM structure of theVibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this proteinin various nucleotide states. These structures show that ParA forms a left-handed filament onDNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rear-rangements upon DNA binding and filament assembly. Collectively, our data suggest thestructural basis for ParA’s cooperative binding to DNA and the formation of high ParA densityregions on the nucleoid.
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700 1 _ |a Mann, Daniel
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700 1 _ |a Tzokov, SB
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700 1 _ |a Hwang, LC
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700 1 _ |a Bergeron, C.
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773 _ _ |a 10.1038/s41467-021-25429-2
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|t Nature Communications
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856 4 _ |u https://juser.fz-juelich.de/record/903486/files/s41467-021-25429-2.pdf
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