Cryo‐<scp>EM</scp> structure of the Min<scp>CD</scp> copolymeric filament from <i>Pseudomonas aeruginosa</i> at 3.1 Å resolution

Harris, Andrzej; Wagstaff, Jane L.; Löwe, Jan

doi:10.1002/1873-3468.13471

Cited by 6 publications

(7 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…MinD forms a dimer, structurally similar to ParA, but does not bind to DNA. Nonetheless, it was recently shown that MinD forms filaments, in the presence of its interacting partner MinC 53 . However, comparison of the MinCD filament to our cryo-EM structure of the ParA2 vc -ATPγS-DNA filament (Supplementary Fig.…”

Section: Discussionmentioning

confidence: 99%

The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding

et al. 2021

View full text Add to dashboard Cite

The efficient segregation of replicated genetic material is an essential step for cell division. Bacterial cells use several evolutionarily-distinct genome segregation systems, the most common of which is the type I Par system. It consists of an adapter protein, ParB, that binds to the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, that binds nonspecific DNA and mediates cargo transport. However, the molecular details of how this system functions are not well understood. Here, we report the cryo-EM structure of the Vibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this protein in various nucleotide states. These structures show that ParA forms a left-handed filament on DNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rearrangements upon DNA binding and filament assembly. Collectively, our data suggest the structural basis for ParA’s cooperative binding to DNA and the formation of high ParA density regions on the nucleoid.

show abstract

Section: Discussionmentioning

confidence: 99%

The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding

et al. 2021

View full text Add to dashboard Cite

show abstract

“…MinC and MinD from E. coli, Pseudomonas aeruginosa , and A. aeolicus readily form copolymers in the presence of ATP composed of alternating dimers ( 13 , 14 , 15 , 16 ). ClpXP is known to disassemble FtsZ polymers in vitro ( 4 , 20 ); therefore, we tested if ClpXP could also prevent assembly of alternating MinCD copolymers or destabilize them after they assemble.…”

Section: Resultsmentioning

confidence: 99%

“…MinC and MinD from several organisms, including E. coli , assemble into ATP-dependent cofilaments in vitro ( 13 , 14 , 15 , 16 ). The Lowe group solved a crystal structure of the Aquifex aeolicus MinCD complex, which supports a model in which A. aeolicus copolymers contain alternating MinC and MinD dimers ( 13 , 14 ).…”

mentioning

confidence: 99%

Degradation of MinD oscillator complexes by Escherichia coli ClpXP

LaBreck

Trebino

Ferreira

et al. 2021

Journal of Biological Chemistry

View full text Add to dashboard Cite

MinD is a cell division ATPase in Escherichia coli that oscillates from pole to pole and regulates the spatial position of the cell division machinery. Together with MinC and MinE, the Min system restricts assembly of the FtsZ-ring to midcell, oscillating between the opposite ends of the cell and preventing FtsZ-ring misassembly at the poles. Here, we show that the ATP-dependent bacterial proteasome complex ClpXP degrades MinD in reconstituted degradation reactions in vitro and in vivo through direct recognition of the MinD N-terminal region. MinD degradation is enhanced during stationary phase, suggesting that ClpXP regulates levels of MinD in cells that are not actively dividing. ClpXP is a major regulator of growth phase–dependent proteins, and these results suggest that MinD levels are also controlled during stationary phase. In vitro , MinC and MinD are known to coassemble into linear polymers; therefore, we monitored copolymers assembled in vitro after incubation with ClpXP and observed that ClpXP promotes rapid MinCD copolymer destabilization and direct MinD degradation by ClpXP. The N terminus of MinD, including residue Arg 3, which is near the ATP-binding site in sequence, is critical for degradation by ClpXP. Together, these results demonstrate that ClpXP degradation modifies conformational assemblies of MinD in vitro and depresses Min function in vivo during periods of reduced proliferation.

show abstract

“…Significantly, ParAB proteins interact with various components of the MinCDE machinery, ParB interacts with MinE, and MinC is a partner of ParA. Pae MinCD proteins organize into filaments at the membranes apart from the midcell, and they may form the scaffold for other proteins to bind there ( 82 ). Interactions with Min proteins may facilitate positioning of ParB- ori complexes in the cells and/or coordinate the cell division process with chromosome segregation ( 3 ).…”

Section: Discussionmentioning

confidence: 99%